3p20

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

spinqualitylabelsall models 3p20, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. Method: X-ray diffraction, Resolution 2.85Å Ligands: ACY, MPD, TRS, VO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AATA_PYRHO Component of the A-type ATP synthase that produces ATP from ADP in the presence of a proton gradient across the membrane. The A chain is the catalytic subunit.[HAMAP-Rule:MF_00309] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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