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3qia

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Revision as of 22:44, 25 December 2014

Crystal structure of P-loop G237A mutant of subunit A of the A1AO ATP synthase

Structural highlights

3qia is a 1 chain structure with sequence from Pyrococcus horikoshii ot3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1vdz, 3i72, 3i73, 3ikj, 3m4y, 3mfy, 3i4l
Gene:	atpA, PH1975 (Pyrococcus horikoshii OT3)
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

The phosphate binding loop (GXXXXGKT(S)) is conserved in several mononucleotide-binding proteins with similar three-dimensional structures. Although variations in other amino acids have been noted, the first glycine and glycine-lysine residues are highly conserved in all enzymes, whose role is yet to be understood. Alanine substitutions for critically positioned glycines-G234, G237, and G239-were generated for the catalytic A-subunit of A-ATP synthase from Pyrococcus horikoshii OT3, and their crystal structures were determined. They showed altered conformation for the phosphate binding loop, with G234A and G237A becoming flat and with G239A taking an intermediate conformation, resulting in the active-site region being closed to nucleotide entry. Furthermore, the essential amino acids S238 and K240, which normally interact with the nucleotide, become inaccessible. These mutant structures demonstrate the role of the strictly conserved glycine residues in guarding the active-site region for nucleotide entrance in archaea-type ATP synthases.

Conserved Glycine Residues in the P-Loop of ATP Synthases Form a Doorframe for Nucleotide Entrance.,Priya R, Kumar A, Manimekalai MS, Gruber G J Mol Biol. 2011 Sep 8. PMID:21925186^[1]

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

References

↑ Priya R, Kumar A, Manimekalai MS, Gruber G. Conserved Glycine Residues in the P-Loop of ATP Synthases Form a Doorframe for Nucleotide Entrance. J Mol Biol. 2011 Sep 8. PMID:21925186 doi:10.1016/j.jmb.2011.08.045

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/3qia"

@@ 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=3qia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qia OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qia RCSB], [http://www.ebi.ac.uk/pdbsum/3qia 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 ==

3qia

From Proteopedia

Revision as of 22:44, 25 December 2014

Crystal structure of P-loop G237A mutant of 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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