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<StructureSection load='RuvBL12_12mer.pdb' size='400' side='right' scene='Journal:JSB:1/Cv/2' caption='Human RuvB-like 1 dodecamer complex with ADP (PDB code [[2c9o]])'>
<StructureSection load='RuvBL12_12mer.pdb' size='400' side='right' scene='Journal:JSB:1/Cv/2' caption='An ATPase, Human RuvB-like 1 dodecamer complex with ADP (PDB code [[2c9o]])'>




[[ATPase]] is an enzyme which catalyzes the breakdown of ATP into ADP and a phosphate ion.  This dephosphorylation releases energy which the enzyme uses to drive other reactions.  ATPAse types include:<br />
[[ATPase]] is an enzyme which catalyzes the breakdown of [[ATP]] into ADP and a phosphate ion.  This dephosphorylation releases energy which the enzyme uses to drive other reactions<ref>PMID:15078220</ref>. The F1/0 ATPase is called '''ATP synthase''' synthesises the reverse reaction, i.e., the addition of phosphate to ADP to form ATP<ref>PMID:30888962</ref>.  ATPase types include:<br />
* '''F-ATPase''' - the prime producers of ATP;<br />
* '''F-ATPase''' - the prime producers of ATP<ref>PMID:8065448</ref>.  For details see [[Alice Clark/ATPsynthase]];<br /> <!--Should there be a F-ATPase page for this like thee is for V-ATPase below? If one is made, I'd like to see links to the animations/movies referenced at https://twitter.com/NathanRoberts17/status/943428752113094656 there.-->
* '''V-ATPase''' or Vacuolar-type H+ ATPase couples the energy to proton transport across membranes.<br />
* '''V-ATPase''' or Vacuolar-type H+ ATPase couples the energy to proton transport across membranes.
* '''A-ATPase''' are found in archaea;<br />
 
* '''P-ATPase''' transport ions;<br />
ATPase is inhibited by [[Bedaquiline]] which is used as TB drug<ref>PMID:28807917</ref>.
* '''E-ATPase''' hydrolyze extracellular ATP.  <br />
 
For details see [[V-ATPase]];<br />
* '''A-ATPase''' are found in archaea.  For details see [[A-ATP Synthase]];<br />
* '''P-ATPase''' transport ions<ref>PMID:20962537</ref><br />
* '''E-ATPase''' hydrolyze extracellular ATP<ref>PMID:7721538</ref>.  <br />
*  '''MipZ''' is an ATPase which forms a complex with the chromosome partitioning protein ParB and is responsible for the regulation of FtsZ ring formation.<br />
*  '''MipZ''' is an ATPase which forms a complex with the chromosome partitioning protein ParB and is responsible for the regulation of FtsZ ring formation.<br />
ATPase domains include metal-binding domain (MBD) and nucleotide-binding domain (NBD). For more details see:<br />
ATPase domains include metal-binding domain (MBD) and nucleotide-binding domain (NBD). For more details see:<br />
*Cu transporting ATPase are in [[P(1B)-Type Cu(I) Transporting ATPases ATP7A and ATP7B]].<br />
* '''ATPase RavA''' participates in the pathway which response to ahminoglycosides under anaerobic conditions and cell membrane regulation<ref>PMID:36127320</ref>.  <br />
*Na/K transporting ATPase are in [[Sodium-Potassium ATPase]].<br />
* '''ATPase InvC''' energizes the apparatus needed for the entry of ''Salmonella typhimurium'' into mammalian cells<ref>PMID:8045880</ref>.  <br />
*H/K transporting ATPase are in [[Esomeprazole and H+/K+ - ATPase Interaction]].<br />
* '''Peroxisomal ATPase''' Pex1/Pex6 is essential for peroxisome formation<ref>PMID:37741838</ref>.  <br />
*Transitional endoplasmic reticulum ATPase are in [[Valosin Containing Protein D120]].<br />
* '''INO8o ATPase''' is a component of the chromatin remodelling complex<ref>PMID:19062292</ref>.  <br />
*Central stalk in F(1)-ATPase is described in [[A-ATP Synthase]].
*'''Cu transporting ATPase''' are in [[P(1B)-Type Cu(I) Transporting ATPases ATP7A and ATP7B]].<br />
*'''Na/K transporting ATPase''' are in [[Sodium-Potassium ATPase]].<br />
*'''H/K transporting ATPase''' are in [[Esomeprazole and H+/K+ - ATPase Interaction]].<br />
*'''Transitional endoplasmic reticulum ATPase''' are in [[Valosin Containing Protein D120]].<br />
*'''Central stalk in F(1)-ATPase''' is described in [[A-ATP Synthase]]<br />
*[[Journal:JSB:1|RuvBL1/RuvBL2 complex (ATPase)]]<br />
 


'''Structural and functional insights into a dodecameric molecular machine – The RuvBL1/RuvBL2 complex (ATPase)<ref >PMID: 21933716</ref>'''<br />
<scene name='Journal:JSB:1/Al/1'>RuvBL1</scene> (RuvB-like 1; [[2c9o]] <ref>PMID: 17060327</ref>; <font color='magenta'><b>colored magenta</b></font>) and its homolog RuvBL2 are evolutionarily highly conserved AAA+ '''ATPases''' essential for many cellular activities. They play an important role in chromatin remodeling, transcriptional regulation and DNA damage repair. RuvBL1 and RuvBL2 are overexpressed in different types of cancer and interact with major oncogenic factors, such as β-catenin and c-myc regulating their function. Since the full-length complex did not crystallize, <scene name='Journal:JSB:1/Al/6'>mutants of RuvBL1 and RuvBL2 with a two-thirds truncation of the flexible domain II</scene> were generated: <scene name='Journal:JSB:1/Al/3'>RuvBL1deltaDII</scene> <font color='darkmagenta'><b>(R1∆DII)</b></font> and <scene name='Journal:JSB:1/Al/5'>RuvBL2deltaDII</scene> <font color='cyan'><b>(R2∆DII)</b></font>. Crystals of the selenomethionine derivative of the R1∆DII/R2∆DII complex diffracted to 3 Å resolution and led to the determination of the three-dimensional structure of the complex. The structure reveals a <scene name='Journal:JSB:1/Cv/2'>dodecamer consisting of two heterohexameric rings with alternating RuvBL1 and RuvBL2 monomers</scene> (the <font color='darkmagenta'><b>RuvBL1</b></font> and the <font color='cyan'><b>RuvBL2</b></font> <scene name='Journal:JSB:1/Cv/3'>monomers in the dodecamer</scene> are colored <font color='darkmagenta'><b>darkmagenta</b></font> and <font color='cyan'><b>cyan</b></font>, respectively) bound to ADP/ATP (click on <scene name='Journal:JSB:1/Cv/5'>RuvBL1 </scene> or, alternatively on <scene name='Journal:JSB:1/Cv/6'>RuvBL2</scene> to see protein/nucleotide interactions). The two heterohexamers interact with each other via the retained part of domain II, which is however poorly visible in the electron density maps, probably because the complex was not crystallized in a single conformational state. This is also hinted by evidence that in the RuvBL1 monomers, ATP was partly hydrolyzed to ADP. The dodecameric quaternary structure of the R1ΔDII/R2ΔDII complex observed in the crystal structure was confirmed by small-angle X-ray scattering analysis. RuvBL1 and RuvBL2 share <scene name='Journal:JSB:1/Al/7'>43 % sequence identity and 65 % sequence similarity and therefore the 3D structures of R1deltaDII and R2deltaDII are very similar</scene>. Due to the low data resolution, and even though the crystal structure could be solved by molecular replacement using a truncated RuvBL1 model, the use of a selenomethionine derivative was essential to elucidate the complex composition, since only one methionine residue is conserved out of 11 in R1ΔDII and 12 in R2ΔDII.
Interestingly, truncation of domain II led to a substantial increase in ATP consumption of RuvBL1, RuvBL2 and their complex. In addition, we present evidence that DNA unwinding of the human RuvBL proteins can be auto-inhibited by domain II, which is not present in the homologous bacterial helicase RuvB. The alternation of charges in the central channel of the dodecamer shown below, combined with the diameter of the channel (ranging between 17 and 21 Å) suggests interactions with single-stranded nucleic acids.
[[Image:Figure_S6.png|left|500px|thumb|Electrostatic potential mapped at the molecular surface for the R1deltaDII/R2deltaDII dodecamer. (a) top view and (b) cross-section view showing the central channel. (c) cross-section view of the SV40 Ltag
hexamer complexed with ATP (PDB [[1svm]]), included for comparison. In (a) and (b) the R1deltaDII and R2deltaDII monomers are colored gold and cyan, respectively. In (c) the SV40 monomers are alternately colored gold and cyan.]]
{{Clear}}
Our data give new insights into the molecular arrangement of RuvBL1 and RuvBL2 and strongly suggest that in vivo activities of these highly interesting therapeutic drug targets are regulated by cofactors inducing conformational changes via domain II in order to modulate the enzyme complex into its active state.


</StructureSection>
</StructureSection>


== 3D Structures of ATPase ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
==3D Printed Physical Model of ATP Synthase==
{{#tree:id=OrganizedByTopic|openlevels=0|


*'''F-ATPase'''
Shown below is a 3D printed physical model of the Respiration Electron Transport Chain. Complex I is colored red, complex II is purple, complex III is green, complex IV is blue and the atp synthase protein is colored orange, yellow and red.
[[Image:atpSynthase1_centerForBioMolecularModeling.jpg |550px]]


*''F1F0 ATPase α subunit''


**[[2jmx]] - bF1-ATPS+subunit O<br />
====The MSOE Center for BioMolecular Modeling====
**[[2r9v]] - F1-ATPS – ''Thermotoga maritima''


*''F1F0 ATPase β subunit''
[[Image:CbmUniversityLogo.jpg | left | 150px]]


**[[1b9u]] – EcF1-ATPS membrane domain – ''Escherichia coli'' -NMR<BR />
The [http://cbm.msoe.edu MSOE Center for BioMolecular Modeling] uses 3D printing technology to create physical models of protein and molecular structures, making the invisible molecular world more tangible and comprehensible. To view more protein structure models, visit our [http://cbm.msoe.edu/educationalmedia/modelgallery/ Model Gallery].
**[[4utq]] – EcF1-ATPS membrane domain + insertase YIDC – Cryo EM<BR />
**[[1l2p]] – EcF1-ATPS dimerization domain<br />
**[[2khk]] - EcF1-ATPS fragment – NMR<BR />
**[[1pyv]] - F1-ATPS – NMR – tobacco<br />
**[[4q4l]] - F1-ATPS – ''Burkholderia thailandensis''<br />


*''F1F0 ATPase γ subunit''
== 3D Structures of ATPase ==
 
[[ATPase 3D structures]]
**[[1wu0]] – BsATPS – NMR<BR />
**[[1a91]], [[1c0v]], [[1aty]], [[1c99]] - EcF1-ATPS – NMR<BR />
**[[2wgm]], [[1yce]] – F0-ATPS – ''Ilyobacter tartaricus''<br />
**[[2x2v]], [[4cbk]], [[4cbj]] – F0-ATPS – ''Bacillus pseudofirmus''<br />
**[[4mjn]] - F1-ATPS - wheat<br />
**[[4bem]] - F1F0-ATPS – ''Acetobacterium woodii''<br />
 
*''F1F0 ATPase δ subunit''
 
**[[1abv]] – EcF1-ATPS N terminal – NMR<BR />
 
*''F1F0 ATPase ε subunit''
 
**[[2rq6]], [[2rq7]] - F1-ATPS – ''Thermosynechococcus elongatus''<br />
**[[1abv]], [[1aqt]] – EcF1-ATPS (mutant)<br />
**[[1bsh]], [[1bsn]] – EcF1-ATPS – NMR<BR />
**[[2e5t]], [[2e5u]] – BsF1-ATPS C terminal – NMR<BR />
**[[2e5y]] – BsF1-ATPS
 
*''F1F0 ATPase α, β subunits''
 
**[1sky]] – BsF1-ATPS – Bacillus sp. Ps3
 
*''F1F0 ATPase α,γ subunits''
 
**[[1c17]] – EcF1-ATPS – NMR<br />
 
*''F1F0 ATPase α, δ subunits''
 
**[[2a7u]] – EcF1-ATPS N termini – NMR<BR />
 
*''F1F0 ATPase β, δ subunits''
 
**[[2cly]] – bF1-ATPS + ATPS coupling factor
 
*''F1F0 ATPase γ, ε subunits''
 
**[[1fs0]] – EcF1-ATPS
 
*''F1F0 ATPase α, β, γ subunits''
 
**[[1ohh]], [[2jiz]], [[4tt3]], [[4tsf]] – bF1-ATPS+ IF1 inhibitor – bovine<br />
**[[1e1q]], [[2w6e]], [[2w6f]], [[2w6g]], [[2w6h]], [[2w6i]], [[2w6j]] - bF1-ATPS<br />
**[[1e1r]] - bF1-ATPS+Mg+ADP+AlF4<br />
**[[1w0j]], [[1w0k]] -  bF1-ATPS+BeF3<br />
**[[1nbm]] -  bF1-ATPS+nitrobenzofurazan<br />
**[[1mab]], [[2f43]] - F1-ATPS – rat
 
*''F1F0 ATPase α,β,γ,δ subunits''
 
**[[1qo1]] - yF1-ATPS + protein 9<br />
 
*''F1F0 ATPase α,β,γ,ε subunits''
 
**[[1jnv]] - EcF1-ATPS <br />
**[[3oaa]] – EcF1-ATPS (mutant)<br />
**[[2qe7]] – F1-ATPS – ''Bacillus''<br />
 
*''F1F0 ATPase α, β, γ, δ, ε subunits''
 
**[[4asu]], [[2jdi]], [[2jj1]], [[2jj2]] - bF1-ATPS<br />
**[[2v7q]], [[1e79]], [[2ck3]] -  bF1-ATPS+inhibitor<br />
**[[2xnd]], [[2xok]] - bF1-ATPS+ATPS lipid-binding protein<br />
**[[2wpd]], [[2wss]] - yF1-ATPS+subunit 9+Mg+ADP+ATP - yeast<br />
**[[3oe7]], [[3oee]], [[3oeh]], [[3ofn]] - yF1-ATPS (mutant)<br />
**[[3fks]], [[3zry]], [[2hld]] - yF1-ATPS<br />
**[[3zia]] - yF1-ATPS + inhibitor protein<br />
**[[3j0j]] – TtATPS α,β,γ,δ,ε,ζ - Cryo EM<br />
**[[1e79]] - bF1-ATPS<br />
 
*''F1F0 ATPase α,β,γ,δ,ε,9,B,D,6,O subunits''
 
**[[4b2q]] – yATPase subunits α,β,γ,δ,ε +9,B,D,6,O – Cryo EM
 
**[[1bmf]] - bF1-ATPS<br />
**[[3dze]] – bF1-ATPS subunit S<br />
**[[1cow]] - bF1-ATPS+aurovertin B<br />
**[[4f4s]] – yATPase subunit 9 + oligomycin <br />
 
*'''V-ATPase'''
 
*''V-ATPase subunit A''
 
**[[3i4l]] - PhATPS subunit A+AMPPNP<br />
**[[3mfy]], [[3m4y]], [[3nd8]], [[3nd9]], [[3p20]], [[3qg1]], [[3qia]], [[3qjy]], [[3sdz]], [[3se0]] - PhATPS subunit A (mutant)<br />
**[[3i72]], [[3i73]], [[3ikj]] - TtATPS subunit A (mutant)<br />
**[[4o1s]] - ATPS subunit A – ''Thermoplasma volcanium''<br />
 
*''V-ATPase subunit B''
 
**[[2c61]] - MmATPS subunit B – ''Methanosarcina mazei''<br />
**[[2rkw]], [[3b2q]], [[3ssa]], [[3tgw]], [[3tiv]] - MmATPS subunit B (mutant)<br />
**[[3dsr]] - MmATPS subunit B+ADP<br />
**[[3eiu]] - MmATPS subunit B+ATP<br />
 
*''V-ATPase subunit C''
 
**[[1u7l]], [[3u2f]], [[3u2y]], [[3u32]], [[3ud0]] - yATPS subunit C<br />
**[[3v3c]] - ATPS subunit C - pea<br />
**[[1ijp]], [[1l6t]] – EcF1-ATPS subunit C (mutant) – ''Escherichia coli'' - NMR<br />
**[[1r5z]], [[1v9m]] - TtATPS subunit C – ''Thermus thermophilus''<br />
**[[3lg8]] - MtATPS subunit C C-terminal<br />
**[[2w5j]] - sATPS subunit C - spinach<br />
**[[2wie]], [[2xqs]], [[2xqt]], [[2xqu]] - ATPS subunit C – ''Arthrospira platensis''<br />
**[[3zk1]], [[3zk2]] - ATPS subunit C – ''Fusobacterium nucleatum''<br />
 
''V-ATPase subunit D+F''
 
**[[4rnd]] – yATPase subunit D+F<br />
 
*''V-ATPase subunit E''
 
**[[2kz9]] – yATPase subunit E<br />
**[[2dm9]], [[2dma]], [[4dt0]] - PhATPS subunit E – ''Pyrococcus horikoshii''<br />
**[[2kk7]] - MjATPS subunit E – ''Methanocaldococcus jannaschii''<br />
**[[3v6i]] – TtATPS subunit E + VAPC<br />
 
*''V-ATPase subunit F''
 
**[[2qai]] - ATPS subunit F – ''Pyrococcus furiosus''<br />
**[[2i4r]] - ATPS subunit F – ''Archaeoglobus fulgidus''<br />
**[[2ov6]] - MmATPS subunit F - NMR<br />
**[[2d00]] - TtATPS subunit F <br />
**[[4ix9]] – yATP subunit F (mutant)<br />
 
*''V-ATPase subunit G''
 
**[[2k88]] - yATPS subunit G - NMR<br />
 
*''V-ATPase subunit H''
 
**[[1ho8]] – yATPS subunit H <br />
 
*''V-ATPase subunit K''
 
**[[2bl2]], [[2cyd]] - ATPS subunit K – ''Enterococcus hirae''<br />
 
*''V-ATPase subunit I''
 
**[[3rrk]] – ATPS subunit I N terminal – ''Meiothermus ruber''
 
**[[4dl0]], [[4efa]] - yATPase subunits C,G,E<br />
**[[3w3a]] - yATPS subunit A,B,D,F<br />
**[[3a5c]], [[3a5d]] - TtATPS subunit A,B,D,F<br />
**[[3gqb]] - TtATPS subunit A (mutant),B (mutant)<br />
**[[3k5b]] - TtATPS subunit E (mutant)+C<br />
 
*'''P-ATPase'''
 
*''Cu transporting ATPase''
 
**[[2kmv]], [[2kmx]], [[2arf]] – hATPase NBD – human – NMR<br />
**[[2kij]] - hATPase actuator domain – NMR<br />
**[[1yjr]], [[1yjt]], [[1yju]], [[1yjv]] - hATPase  (mutant) 6th soluble domain – NMR<br />
**[[1y3j]], [[1y3k]] - hATPase  5th soluble domain – NMR<br />
**[[1s6o]], [[1s6u]] - hATPase  2nd soluble domain – NMR<br />
**[[1q8l]] - hATPase  2nd MBD  – NMR<br />
**[[1aw0]], [[2aw0]] - hATPase  4th MBD  – NMR<br />
**[[1kvi]], [[1kvj]] - hATPase  1st MBD  – NMR<br />
**[[3dxs]] - AtATPase MBD – ''Arabidopsis thaliana''<br />
**[[3voy]] - AfATPase – Archaeoglobus fulgidus – CryoEM<br />
**[[3skx]], [[3sky]] - AfATPase NBD<br />
**[[2k1r]] - hATPase MBD+ ATOX1 – NMR<br />
**[[2rop]], [[2g9o]], [[2ga7]] - hATPase MBD – NMR<br />
**[[2rml]] - BsATPase N-terminal – ''Bacillus subtilis'' – NMR<br />
**[[2gcf]] - sATPase N-terminal - ''Synechocystis'' – NMR<br />
**[[4a48]] - sATPase<br />
**[[2iye]] - SsATPase catalytic domain – ''Sulfolobus solfataricus''<br />
**[[2yj3]] - SsATPase catalytic domain (mutant)<br />
**[[2yj4]], [[2yj5]], [[2yj6]] - SsATPase catalytic domain (mutant) + nucleotide<br />
**[[1fvq]], [[1fvs]] - hATPase – NMR<br />
**[[3cjk]] – hATPase + Cu transporting protein ATX1<br />
**[[3rfu]] – ATPase – ''Legionella pneumophila''<br />
**[[4f2f]] - ATPase metal-binding domain – ''Streptococcus pneumonia''<br />
**[[3j08]], [[3j09]] - AfATPase<br />
**[[3a1c]] – AfATPase + AMPPCP<br />
**[[3a1d]] - AfATPase + ADP-Mg<br / >
**[[3a1e]] - AfATPase (mutant) + AMPPCP<br />
 
*''Na/K transporting ATPase''
 
**[[3a3y]] - SaATPase+K+ouabain – ''Squalus acanthias''<br />
**[[3kdp]], [[3b8e]] – pATPase  – pig <br />
**[[3n23]] – pATPase + ouabain<br />
**[[3wgv]], [[3wgu]] – pATPase + oligomycin<br />
**[[3b8e]] - pATPase a+BeF3 <br />
**[[2hc8]] –AfATPase CopA A domain<br />
**[[2b8e]] - AfATPase CopA NBD<br />
**[[2xze]] - SaATPase<br />
**[[1mo8]], [[1mo7]] - ATPase α-1 – rat<br />
**[[1q3i]] - pATPase NBD<br />
**[[3n2f]], [[4ret]], [[4res]], [[4hyt]], [[4hqj]] - pATPase subunits α,β,γ<br />
**[[2zxe]] - ATPase subunits α,β + phospholemman-like protein – spiny dogfish
 
*''Ca+2 transporting ATPase''
 
**[[3fgo]] - rATPase+CPA+AMPPCP – rabbit<br />
**[[3b9r]], [[1xp5]] - rATPase+AlF4<br />
**[[1wpg]] - rATPase+MgF4<br />
**[[3w5b]] - rATPase+Mg<br />
**[[4h1w]], [[3w5a]] - rATPase+ sarcolipin<br />
**[[3w5c]], [[3w5d]], [[1iwo]] - rATPase<br />
**[[4bew]] - rATPase+ phosphate analog<br />
**[[2zbe]], [[3b9b]] – rATPase+BeF3<br />
**[[2zbf]] - rATPase+BeF3+TG<br />
**[[2zbg]] - rATPase+AlF4+TG<br />
**[[2zbd]], [[3ar8]] - rATPase+AlF4+nucleotide+Ca<br />
**[[3ar9]] - rATPase+BeF3+nucleotide<br />
**[[2dqs]], [[3ar2]], [[1vfp]]  - rATPase+AMPPCP<br />
**[[2c88]], [[2c8k]], [[3ar4]], [[3ar3]], [[3ar5]], [[3ar7]] - rATPase+nucleotide+TG<br />
**[[2ear]], [[2c8l]] - rATPase+TG<br />
**[[2agv]] - rATPase+TG+BHQ<br />
**[[2eas]] - rATPase+CPA<br />
**[[2eat]] - rATPase+CPA+GT<br />
**[[3ar6]] - rATPase+TNP-ADP+GT<br />
**[[2eau]] - rATPase+CPA+curcumin<br />
**[[3ba6]] - rATPase phosphoenzyme intermediate<br />
**[[3fpb]] - rATPase+ATP+cyclopiazonic acid<br />
**[[3fps]], [[2oa0]] - rATPase+ADP+cyclopiazonic acid<br />
**[[2o9j]] - rATPase+MgF4+cyclopiazonic acid<br />
**[[1kju]], [[3n5k]] - rATPase E2 state<br />
**[[2c9m]] - rATPase Ca2E1 state<br />
**[[1t5s]], [[3n8g]] - rATPase Ca2E1 state+AMPPCP<br />
**[[4nab]] - rATPase Ca2E1 state (mutant) +AMPPCP<br />
**[[1t5t]] - rATPase Ca2E1 state+ADP+AlF4<br />
**[[1su4]] - rATPase +2Ca2<br />
**[[2by4]], [[2yfy]], [[3nal]], [[3nam]], [[3nan]], [[4uu1]], [[4uu0]], [[4j2t]] - rATPase HNE2 state+thapsigargin derivative
 
*''Zn+2 transporting ATPase''
 
**[[2ofg]], [[2ofh]] - sATPase N-terminal – NMR<br />
**[[4umw]], [[4umv]] - ATPase +Mg – Shigella sonni<br />
 
*''K+ transporting ATPase''
 
**[[2a00]], [[2a29]] - EcATPase NBD of KdpB+AMPPNP– ''Escherichia coli'' – NMR<br />
**[[1svj]], [[1u7q]] - EcATPase NBD of KdpB – NMR<br />
**[[2ynr]] – pATPase – Cryo EM
 
*''As+ transporting ATPase''
 
**[[1ii0]], [[1f48]] - EcATPase<br />
**[[1ihu]] – EcATPase+Mg+ADP+AlF3<br />
**[[1ii9]] - EcATPase<br />
**[[3h84]], [[3idq]],  [[3a36]], [[3a37]] - yATPase GET3 – yeast<br />
**[[3sja]], [[3sjb]], [[3sjc]], [[3sjd]], [[3zs8]], [[3zs9]], [[3b2e]], [[3vlc]] - yATPase GET3 + GET1 cystolic domain<br />
**[[3ibg]] - ATPase GET3 – ''Aspergillus fumigatus''
 
*''H+ transporting ATPase''
 
**[[3b8c]]  - AtATPase C terminal truncated<br />
**[[1mhs]] - ATPase – ''Neurospora crassa''<br />
 
*''Na+ transporting ATPase''
 
**[[2db4]], [[3aou]] - EhATPase subunit K – ''Enterococcus hirae''<br />
**[[3aon]] - EhATPase subunits D,G<br />
**[[3vr2]] - EhATPase subunits A,B<br />
**[[3vr4]], [[3vr5]] - EhATPase subunits A,B,D,G<br />
**[[3vr3]] - EhATPase subunits A,B + AMPPNP<br />
**[[3vr6]] - EhATPase subunits A,B,D,G + AMPPNP<br />
**[[1yce]] - ATPase rotor ring – ''Ilyobacter tartaricus''
 
*''H/K transporting ATPase''
 
**[[1iwc]], [[1iwf]] - pATPase NBD <br />
**[[3ixz]] - pATPase a+AlF4<br />
**[[2xzb]] – pATPase subunits α, β<br />
 
*''Mg+2 transporting ATPase''
 
**[[3gwi]] – EcATPase P-1 NBD
 
*''Arg/ornithine transporting ATPase''
 
**[[3md0]] – MtATPase+GDP – ''Mycobacterium tuberculosis''<br />
**[[1kmh]] - ATPase alpha subunit+tentoxin – spinach<br />
**[[1h8e]] – cATPase+ADP+AlF4+ADP+SO4 - cow<br />
**[[1h8h]] - cATPase+ AMPPNP<br />
**[[1efr]] - cATPase+efrapeptin<br />
**[[3fks]] – ATPase – yeast<br />
**[[3ea0]] – ATPase ParA, fragment – ''Chlorobium tepidum''<br />
**[[2qen]] – ATPase (mutant) Walker-type – ''Pyrococcus abyssi''<br />
**[[3cf0]], [[3cf1]], [[3cf3]] – mATPase  NBD+ADP – mouse<br />
**[[3cf2]] - mATPase NBD+ADP+AMP-PNP<br />
**[[2r31]], [[2p4x]] – PdATPase ATP12 – ''Paracoccus denitrificans''<br />
**[[2zd2]] – PdATPase (mutant) ATP12<br />
**[[1d8s]] – EcATPase F1<br />
**[[1vdz]] – PhATPase subunit A – ''Pyrococcus horikoshii''<br />
 
*'''RNA-dependent ATPase'''
 
**[[3eaq]], [[3i31]], [[3i32]] – TtATPase fragment<br />
**[[3mwj]] – TtATPase N-terminal (mutant)<br />
**[[3mwk]], [[3nbf]] – TtATPase N-terminal + 8-oxo-AMP<br />
**[[3mwl]] - TtATPase N-terminal (mutant) + 8-oxoadenine<br />
**[[3nej]] - TtATPase reca-like domain (mutant)
 
*'''Proteasome-associated ATPase'''
 
**[[3fp9]], [[3m9b]], [[3m9h]] – MtATPase intern domain<br />
**[[3m91]], [[3m9d]] - MtATPase coiled coil domain + protein PUP<br />
**[[3kw6]] – hATPase 5
 
*'''Transitional endoplasmic reticulum ATPase'''
 
**[[3hu1]], [[3hu2]], [[3hu3]] – hTer-ATPase + ATPGS<br />
**[[3qc8]], [[3qq8]], [[3qwz]] - hTer-ATPase N terminal + FAS-associated factor 1<br />
**[[3qq7]] - hTer-ATPase N terminal<br />
**[[3tiw]] - hTer-ATPase N terminal + E3 ubiquitin-protein ligase peptide
 
*'''LAO/AO transport system ATPase'''
 
**[[3nxs]] – ATPase – ''Mycobacterium smegmatis''
 
*'''DNA double-strand repair ATPase (Rad50)'''
 
**[[3aux]] – MjRad50 – ''Methanocaldococcus jannaschii''<br />
**[[3auy]] - MjRad50 + ADP<br />
**[[3av0]] - MjRad50 + ATP<br />
**[[3qg5]] – Rad50 NBD + MRE11 – ''Thermotoga maritima''<br />
**[[3qkr]], [[3qks]], [[3qf7]] - PfRad50 NBD + MRE11 – ''Pyrococcus furiosus''<br />
**[[3qkt]] - PfRad50 NBD + AMPPNP<br />
**[[3qku]] - PfRad50 NBD + AMPPNP + MRE11
 
*'''MipZ ATPase'''
 
**[[2xit]], [[2xj4]] – CcMipZ – ''Caulobacter crescentus''<br />
**[[2xj9]] – CcMipZ (mutant)
 
 
**[[3nbx]] – EcATPase Rava + ADP
 
*'''FlaI ATPase'''


**[[4ihq]], [[4ii7]] – ATPase (mutant) – ''Sulfolobus acidocaldarius''<br />
}}
==References==
==References==
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[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky, Michal Harel, Wayne Decatur, Mark Hoelzer, Karsten Theis
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