3lg8
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Crystal structure of the C-terminal part of subunit E (E101-206) from Methanocaldococcus jannaschii of A1AO ATP synthase
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Structural highlights
FunctionVATE_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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 16:23, 1 November 2023.