3eiu

A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A1Ao ATP synthase

spinqualitylabelsall models 3eiu, resolution 3.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3eiu is a 2 chain structure with sequence from Methanosarcina mazei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.43Å Ligands: AES, ATP 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The adenosine triphosphate (ATP) entrance into the nucleotide-binding subunits of ATP synthases is a puzzle. In the previously determined structure of subunit B mutant R416W of the Methanosarcina mazei Go1 A-ATP synthase one ATP could be trapped at a transition position, close to the phosphate-binding loop. Using defined parameters for co-crystallization of an ATP-bound B-subunit, a unique transition position of ATP could be found in the crystallographic structure of this complex, solved at 3.4 A resolution. The nucleotide is found near the helix-turn-helix motif in the C-terminal domain of the protein; the location occupied by the gamma-subunit to interact with the empty beta-subunit in the thermoalkaliphilic Bacillus sp. TA2.A1 of the related F-ATP synthase. When compared with the determined structure of the ATP-transition position, close to the P-loop, and the nucleotide-free form of subunit B, the C-terminal domain of the B mutant is rotated by around 6 degrees, implicating an ATP moving pathway. We propose that, in the nucleotide empty state the central stalk subunit D is in close contact with subunit B and when the ATP molecule enters, D moves slightly, paving way for it to interact with the subunit B, which makes the C-terminal domain rotate by 6 degrees. A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A(1)A(0) ATP synthase.,Manimekalai MS, Kumar A, Balakrishna AM, Gruber G J Struct Biol. 2009 Apr;166(1):38-45. Epub 2008 Dec 24. PMID:19138746 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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