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3p20

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Revision as of 15:16, 25 December 2014

Crystal structure of vanadate bound subunit A of the A1AO ATP synthase

Structural highlights

3p20 is a 1 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	3i72, 3i4l, 3ikj, 3i73, 3m4y, 3mfy
Gene:	atpA, PH1975 (Pyrococcus horikoshii)
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[VATA_PYRHO] Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.

Publication Abstract from PubMed

Archaeal A-ATP synthases catalyze the formation of the energy currency ATP. The chemical mechanisms of ATP synthesis in A-ATP synthases are unknown. We have solved the crystal structure of a transition-like state of the vanadate-bound form of catalytic subunit A (A(Vi)) of the A-ATP synthase from Pyrococcus horikoshii OT3. Two orthovanadate molecules were observed in the A(Vi) structure, one of which interacts with the phosphate binding loop through residue S238. The second vanadate is positioned in the transient binding site, implicating for the first time the pathway for phosphate entry to the catalytic site. Moreover, since residues K240 and T241 are proposed to be essential for catalysis, the mutant structures of K240A and T241A were also determined. The results demonstrate the importance of these two residues for transition-state stabilization. The structures presented shed light on the diversity of catalytic mechanisms used by the biological motors A- and F-ATP synthases and eukaryotic V-ATPases.

The Transition-Like State and P(i) Entrance into the Catalytic A Subunit of the Biological Engine A-ATP Synthase.,Manimekalai MS, Kumar A, Jeyakanthan J, Gruber G J Mol Biol. 2011 Mar 16. PMID:21396943^[1]

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

References

↑ Manimekalai MS, Kumar A, Jeyakanthan J, Gruber G. The Transition-Like State and P(i) Entrance into the Catalytic A Subunit of the Biological Engine A-ATP Synthase. J Mol Biol. 2011 Mar 16. PMID:21396943 doi:10.1016/j.jmb.2011.03.010

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3p20"

@@ Line 9: / Line 9: @@
 <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=3p20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p20 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p20 RCSB], [http://www.ebi.ac.uk/pdbsum/3p20 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/VATA_PYRHO VATA_PYRHO]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3p20

From Proteopedia

Revision as of 15:16, 25 December 2014

Crystal structure of vanadate bound subunit A of the A1AO ATP synthase

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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