3lg8 | pdb_00003lg8

Crystal structure of the C-terminal part of subunit E (E101-206) from Methanocaldococcus jannaschii of A1AO ATP synthase

spinqualitylabelsall models 3lg8, resolution 4.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lg8 is a 2 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 4.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VATE_METJA Produces ATP from ADP in the presence of a proton gradient across the membrane (By similarity). 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 structure of the C-terminus of subunit E (E(101-206)) of Methanocaldococcus jannaschii A-ATP synthase was determined at 4.1 A. E(101-206) consist of a N-terminal globular domain with three alpha-helices and four antiparallel beta-strands and an alpha-helix at the very C-terminus. Comparison of M. jannaschii E(101-206) with the C-terminus E(81-198) subunit E from Pyrococcus horikoshii OT3 revealed that the kink in the C-terminal alpha-helix of E(81-198), involved in dimer formation, is absent in M. jannaschii E(101-206). Whereas a major dimeric surface interface is present between the P. horikoshii E(81-198) molecules in the asymmetric unit, no such interaction could be found in the M. jannaschii E(101-206) molecules. To verify the oligomeric behaviour, the low resolution structure of the recombinant E(85-206) from M. jannaschii was determined using small angle X-ray scattering. Rigid body modeling of two copies of one of the monomer established a fit with a tail to tail arrangement. Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A(1)A (O) ATP synthase subunit E revealed by X-ray diffraction and small-angle X-ray scattering.,Balakrishna AM, Manimekalai MS, Hunke C, Gayen S, Rossle M, Jeyakanthan J, Gruber G J Bioenerg Biomembr. 2010 Jun 23. PMID:20571891 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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