2K88

Association of subunit d (Vma6p) and E (Vma4p) with G (Vma10p) and the NMR solution structure of subunit G (G1-59) of the Saccharomyces cerevisiae V1VO ATPase

Summary for 2K88

• Entry DOI: 10.2210/pdb2k88/pdb
• Descriptor: Vacuolar proton pump subunit G (1 entity in total)
• Functional Keywords: g subunit, v1vo atpase, vma10p, hydrogen ion transport, hydrolase, ion transport, transport
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• Total number of polymer chains: 1
• Total formula weight: 6969.02

Authors

Sankaranarayanan, N.,Gayen, S.,Thaker, Y.,Subramanian, V.,Manimekalai, M.S.S.,Gruber, G. (deposition date: 2008-09-04, release date: 2009-08-11, Last modification date: 2024-05-22)

Primary citation

Rishikesan, S.,Gayen, S.,Thaker, Y.R.,Vivekanandan, S.,Manimekalai, M.S.,Yau, Y.H.,Shochat, S.G.,Gruber, G.
Assembly of subunit d (Vma6p) and G (Vma10p) and the NMR solution structure of subunit G (G(1-59)) of the Saccharomyces cerevisiae V(1)V(O) ATPase.
Biochim.Biophys.Acta, 1787:242-251, 2009

PubMed Abstract: Understanding the structural traits of subunit G is essential, as it is needed for V(1)V(O) assembly and function. Here solution NMR of the recombinant N- (G(1-59)) and C-terminal segment (G(61-114)) of subunit G, has been performed in the absence and presence of subunit d of the yeast V-ATPase. The data show that G does bind to subunit d via its N-terminal part, G(1-59) only. The residues of G(1-59) involved in d binding are Gly7 to Lys34. The structure of G(1-59) has been solved, revealing an alpha-helix between residues 10 and 56, whereby the first nine- and the last three residues of G(1-59) are flexible. The surface charge distribution of G(1-59) reveals an amphiphilic character at the N-terminus due to positive and negative charge distribution at one side and a hydrophobic surface on the opposite side of the structure. The C-terminus exhibits a strip of negative residues. The data imply that G(1-59)-d assembly is accomplished by hydrophobic interactions and salt-bridges of the polar residues. Based on the recently determined NMR structure of segment E(18-38) of subunit E of yeast V-ATPase and the presently solved structure of G(1-59), both proteins have been docked and binding epitopes have been analyzed.

PubMed: 19344662
DOI: 10.1016/j.bbabio.2009.01.010

Experimental method

SOLUTION NMR