title: NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.
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.
authors.affiliation: School of Biological Sciences, Nanyang Technological University, Singapore, Republic of Singapore.
authors.forename: Sankaranarayanan
authors.initials: S
authors.lastname: Rishikesan
authors.forename: Youg R
authors.initials: YR
authors.lastname: Thaker
authors.forename: Gerhard
authors.initials: G
authors.lastname: Grüber
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D029701:Saccharomyces cerevisiae Proteins; C447617:VMA13 protein, S cerevisiae; C500733:Vma4 protein, S cerevisiae; C485339:VMA10 protein, S cerevisiae; D025262:Vacuolar Proton-Translocating ATPases