1abv

N-TERMINAL DOMAIN OF THE DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI, NMR, MINIMIZED AVERAGE STRUCTURE

spinqualitylabelsall models 1abv, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1abv is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ATPD_ECOLI] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.[HAMAP-Rule:MF_01416] This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.[HAMAP-Rule:MF_01416] 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 NMR studies of the delta subunit of the Escherichia coli F1F0-ATPsynthase reveal that it consists of an N-terminal six alpha-helix bundle and a less well ordered C terminus. Both domains are part of one of two separate connections between F1 and F0. Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase.,Wilkens S, Dunn SD, Chandler J, Dahlquist FW, Capaldi RA Nat Struct Biol. 1997 Mar;4(3):198-201. PMID:9164460 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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