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    J Bioenerg Biomembr. 2011 Apr;43(2):187-93. doi: 10.1007/s10863-011-9342-y. Epub 2011 Mar 12.

    NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.

    Rishikesan S, Thaker YR, Grüber G.

    Source

    School of Biological Sciences, Nanyang Technological University, Singapore, Republic of Singapore.

    Abstract

    The N-terminus of V-ATPase subunit E has been shown to associate with the subunits C, G and H, respectively. To understand the assembly of E with its neighboring subunits as well as its N-terminal structure, the N-terminal region, E(1-69), of the Saccharomyces cerevisiae V-ATPase subunit E was expressed and purified. The solution structure of E(1-69) was determined by NMR spectroscopy. The protein is 90.3 Å in length and forms an á-helix between the residues 12-68. The molecule is amphipathic with hydrophobic residues at the N-terminus, predicted to interact with subunit C. The polar epitopes of E(1-69) are discussed as areas interacting with subunits G and H.

    PMID:
    21399923
    [PubMed - indexed for MEDLINE]

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