| Literature DB >> 21399923 |
Sankaranarayanan Rishikesan1, Youg R Thaker, Gerhard Grüber.
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.Entities:
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Year: 2011 PMID: 21399923 DOI: 10.1007/s10863-011-9342-y
Source DB: PubMed Journal: J Bioenerg Biomembr ISSN: 0145-479X Impact factor: 2.945