Crystal structure of subunits D and F in complex gives insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae

Asha Manikkoth Balakrishna, Sandip Basak, Malathy Sony Subramanian Manimekalai, Gerhard Grüber*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)

Abstract

Background: Subunits D and F are essential in ATP hydrolysis and reversible disassembly of V1VO-ATPases. Results: First crystallographic structure of eukaryotic V-ATPase subunit D and entire subunit F is presented. Conclusion: Structural elements in subunits D and F enable the DF assembly to become a central motor element in the engine V-ATPase. Significance: Mechanistic understanding of the subunit DF assembly and its key roles in enzyme catalysis and regulation are presented.

Original languageEnglish
Pages (from-to)3183-3196
Number of pages14
JournalJournal of Biological Chemistry
Volume290
Issue number6
DOIs
Publication statusPublished - Feb 6 2015
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

ASJC Scopus Subject Areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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