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5bqa

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Revision as of 14:28, 12 October 2017

Structure of the yeast F1FO ATPase C10 ring with oligomycin C

Structural highlights

5bqa is a 10 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	5bps, 5bq6, 5bqj
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ATP9_YEAST] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

Publication Abstract from PubMed

We report the high-resolution (1.9 A) crystal structure of oligomycin bound to the subunit c(10) ring of the yeast mitochondrial ATP synthase. Oligomycin binds to the surface of the c(10) ring making contact with two neighboring molecules at a position that explains the inhibitory effect on ATP synthesis. The carboxyl side chain of Glu59, which is essential for proton translocation, forms an H-bond with oligomycin via a bridging water molecule but is otherwise shielded from the aqueous environment. The remaining contacts between oligomycin and subunit c are primarily hydrophobic. The amino acid residues that form the oligomycin-binding site are 100% conserved between human and yeast but are widely different from those in bacterial homologs, thus explaining the differential sensitivity to oligomycin. Prior genetics studies suggest that the oligomycin-binding site overlaps with the binding site of other antibiotics, including those effective against Mycobacterium tuberculosis, and thereby frames a common "drug-binding site." We anticipate that this drug-binding site will serve as an effective target for new antibiotics developed by rational design.

Oligomycin frames a common drug-binding site in the ATP synthase.,Symersky J, Osowski D, Walters DE, Mueller DM Proc Natl Acad Sci U S A. 2012 Aug 6. PMID:22869738^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Symersky J, Osowski D, Walters DE, Mueller DM. Oligomycin frames a common drug-binding site in the ATP synthase. Proc Natl Acad Sci U S A. 2012 Aug 6. PMID:22869738 doi:10.1073/pnas.1207912109

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5bqa"

@@ Line 1: / Line 1: @@
 ==Structure of the yeast F1FO ATPase C10 ring with oligomycin C==
 <StructureSection load='5bqa' size='340' side='right' caption='[[5bqa]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bps|5bps]], [[5bq6|5bq6]], [[5bqj|5bqj]]</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=5bqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bqa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bqa RCSB], [http://www.ebi.ac.uk/pdbsum/5bqa PDBsum]</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=5bqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bqa OCA], [http://pdbe.org/5bqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bqa RCSB], [http://www.ebi.ac.uk/pdbsum/5bqa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bqa ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 5bqa" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

5bqa

From Proteopedia

Revision as of 14:28, 12 October 2017

Structure of the yeast F1FO ATPase C10 ring with oligomycin C

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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