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==AAA ATPase domain of the proteasome- activating nucleotidase==
==AAA ATPase domain of the proteasome- activating nucleotidase==
<StructureSection load='3h4m' size='340' side='right' caption='[[3h4m]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
<StructureSection load='3h4m' size='340' side='right'caption='[[3h4m]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3h4m]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H4M FirstGlance]. <br>
<table><tr><td colspan='2'>[[3h4m]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H4M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.106&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h43|3h43]], [[3h4p|3h4p]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pan, MJ1176 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h4m OCA], [https://pdbe.org/3h4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h4m RCSB], [https://www.ebi.ac.uk/pdbsum/3h4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h4m ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3h4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h4m OCA], [http://pdbe.org/3h4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h4m RCSB], [http://www.ebi.ac.uk/pdbsum/3h4m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h4m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PAN_METJA PAN_METJA]] ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates. In addition to ATP, is able to cleave other nucleotide triphosphates such as CTP, GTP and UTP, but hydrolysis of these other nucleotides is less effective in promoting proteolysis than ATP. Moreover, PAN by itself can function as a chaperone in vitro.[HAMAP-Rule:MF_00553]<ref>PMID:10473546</ref> <ref>PMID:10692374</ref> <ref>PMID:16337593</ref> <ref>PMID:17803938</ref> <ref>PMID:19481528</ref>
[https://www.uniprot.org/uniprot/PAN_METJA PAN_METJA] ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates. In addition to ATP, is able to cleave other nucleotide triphosphates such as CTP, GTP and UTP, but hydrolysis of these other nucleotides is less effective in promoting proteolysis than ATP. Moreover, PAN by itself can function as a chaperone in vitro.[HAMAP-Rule:MF_00553]<ref>PMID:10473546</ref> <ref>PMID:10692374</ref> <ref>PMID:16337593</ref> <ref>PMID:17803938</ref> <ref>PMID:19481528</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h4m ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3h4m ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Eukaryotic proteasome consists of a core particle (CP), which degrades unfolded protein, and a regulatory particle (RP), which is responsible for recognition, ATP-dependent unfolding, and translocation of polyubiquitinated substrate protein. In the archaea Methanocaldococcus jannaschii, the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). Here, we report the crystal structures of essential elements of the archaeal proteasome: the CP, the ATPase domain of PAN, and a distal subcomplex that is likely the first to encounter substrate. The distal subcomplex contains a coiled-coil segment and an OB-fold domain, both of which appear to be conserved in the eukaryotic proteasome. The OB domains of PAN form a hexameric ring with a 13 A pore, which likely constitutes the outermost constriction of the substrate translocation channel. These studies reveal structural codes and architecture of the complete proteasome, identify potential substrate-binding sites, and uncover unexpected asymmetry in the RP of archaea and eukaryotes.
Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii.,Zhang F, Hu M, Tian G, Zhang P, Finley D, Jeffrey PD, Shi Y Mol Cell. 2009 May 14;34(4):473-84. PMID:19481527<ref>PMID:19481527</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3h4m" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43067]]
[[Category: Large Structures]]
[[Category: Finley, D]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Hu, M]]
[[Category: Finley D]]
[[Category: Jeffrey, P]]
[[Category: Hu M]]
[[Category: Shi, Y]]
[[Category: Jeffrey P]]
[[Category: Tian, G]]
[[Category: Shi Y]]
[[Category: Zhang, F]]
[[Category: Tian G]]
[[Category: Zhang, P]]
[[Category: Zhang F]]
[[Category: Atp-binding]]
[[Category: Zhang P]]
[[Category: Atpase]]
[[Category: Hydrolase]]
[[Category: Nucleotide-binding]]
[[Category: Pan]]
[[Category: Proteasome]]

Latest revision as of 12:58, 21 February 2024

AAA ATPase domain of the proteasome- activating nucleotidaseAAA ATPase domain of the proteasome- activating nucleotidase

Structural highlights

3h4m is a 3 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.106Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAN_METJA ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates. In addition to ATP, is able to cleave other nucleotide triphosphates such as CTP, GTP and UTP, but hydrolysis of these other nucleotides is less effective in promoting proteolysis than ATP. Moreover, PAN by itself can function as a chaperone in vitro.[HAMAP-Rule:MF_00553][1] [2] [3] [4] [5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Zwickl P, Ng D, Woo KM, Klenk HP, Goldberg AL. An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes. J Biol Chem. 1999 Sep 10;274(37):26008-14. PMID:10473546
  2. ↑ Wilson HL, Ou MS, Aldrich HC, Maupin-Furlow J. Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome. J Bacteriol. 2000 Mar;182(6):1680-92. PMID:10692374
  3. ↑ Smith DM, Kafri G, Cheng Y, Ng D, Walz T, Goldberg AL. ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins. Mol Cell. 2005 Dec 9;20(5):687-98. PMID:16337593 doi:http://dx.doi.org/10.1016/j.molcel.2005.10.019
  4. ↑ Smith DM, Chang SC, Park S, Finley D, Cheng Y, Goldberg AL. Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry. Mol Cell. 2007 Sep 7;27(5):731-44. PMID:17803938 doi:10.1016/j.molcel.2007.06.033
  5. ↑ Zhang F, Wu Z, Zhang P, Tian G, Finley D, Shi Y. Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Mol Cell. 2009 May 14;34(4):485-96. doi: 10.1016/j.molcel.2009.04.022. PMID:19481528 doi:http://dx.doi.org/10.1016/j.molcel.2009.04.022

3h4m, resolution 3.11Å

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