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==Crystal structure of subunit B mutant N157T of the A1AO ATP synthase==
==Crystal structure of subunit B mutant N157T of the A1AO ATP synthase==
<StructureSection load='3ssa' size='340' side='right' caption='[[3ssa]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3ssa' size='340' side='right'caption='[[3ssa]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ssa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SSA FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ssa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei_Go1 Methanosarcina mazei Go1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SSA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=AES:4-(2-AMINOETHYL)BENZENESULFONYL+FLUORIDE'>AES</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b2q|3b2q]], [[3dsr|3dsr]], [[3eiu|3eiu]], [[2c61|2c61]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=AES:4-(2-AMINOETHYL)BENZENESULFONYL+FLUORIDE'>AES</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ahaB, atpB, MM_0779 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2209 Methanosarcina mazei])</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=3ssa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ssa OCA], [https://pdbe.org/3ssa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ssa RCSB], [https://www.ebi.ac.uk/pdbsum/3ssa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ssa ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </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=3ssa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ssa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ssa RCSB], [http://www.ebi.ac.uk/pdbsum/3ssa PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VATB_METMA VATB_METMA]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.  
[https://www.uniprot.org/uniprot/VATB_METMA VATB_METMA] Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A strategically placed tryptophan in position of Arg416 was used as an optical probe to monitor adenosine triphosphate and adenosine-diphosphate binding to subunit B of the A(1)A(O) adenosine triphosphate (ATP) synthase from Methanosarcina mazei Go1. Tryptophan fluorescence and fluorescence correlation spectroscopy gave binding constants indicating a preferred binding of ATP over ADP to the protein. The X-ray crystal structure of the R416W mutant protein in the presence of ATP was solved to 2.1 A resolution, showing the substituted Trp-residue inside the predicted adenine-binding pocket. The cocrystallized ATP molecule could be trapped in a so-called transition nucleotide-binding state. The high resolution structure shows the phosphate residues of the ATP near the P-loop region (S150-E158) and its adenine ring forms pi-pi interaction with Phe149. This transition binding position of ATP could be confirmed by tryptophan emission spectra using the subunit B mutant F149W. The trapped ATP position, similar to the one of the binding region of the antibiotic efrapeptin in F(1)F(O) ATP synthases, is discussed in light of a transition nucleotide-binding state of ATP while on its way to the final binding pocket. Finally, the inhibitory effect of efrapeptin C in ATPase activity of a reconstituted A(3)B(3)- and A(3)B(R416W)(3)-subcomplex, composed of subunit A and the B subunit mutant R416W, of the A(1)A(O) ATP synthase is shown.
 
Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A1Ao ATP synthase.,Kumar A, Manimekalai MS, Balakrishna AM, Hunke C, Weigelt S, Sewald N, Gruber G Proteins. 2009 Jun;75(4):807-19. PMID:19003877<ref>PMID:19003877</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[ATPase|ATPase]]
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Methanosarcina mazei]]
[[Category: Large Structures]]
[[Category: Gruber, G]]
[[Category: Methanosarcina mazei Go1]]
[[Category: Jeyakanthan, J]]
[[Category: Gruber G]]
[[Category: Manimekalai, M S.S]]
[[Category: Jeyakanthan J]]
[[Category: Sundararaman, L]]
[[Category: Manimekalai MSS]]
[[Category: Atp binding]]
[[Category: Sundararaman L]]
[[Category: Hydrolase]]

Latest revision as of 20:26, 1 November 2023

Crystal structure of subunit B mutant N157T of the A1AO ATP synthaseCrystal structure of subunit B mutant N157T of the A1AO ATP synthase

Structural highlights

3ssa is a 2 chain structure with sequence from Methanosarcina mazei Go1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VATB_METMA Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.

See Also

3ssa, resolution 1.70Å

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