| Autor: |
Rishikesan, Sankaranarayanan, Thaker, Youg R., Grüber, Gerhard |
| Předmět: |
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| Zdroj: |
Journal of Bioenergetics & Biomembranes; Apr2011, Vol. 43 Issue 2, p187-193, 7p, 2 Diagrams, 1 Chart, 2 Graphs |
| Abstrakt: |
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, of the Saccharomyces cerevisiae V-ATPase subunit E was expressed and purified. The solution structure of E 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 are discussed as areas interacting with subunits G and H. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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