Structural features and nucleotide-binding capability of the C subunit are integral to the regulation of the eukaryotic V1V0 ATPases

Biochemical Society Transactions

Volumn 33, Issue 4, 2005, Pages 883-885

  Gruber G ^a,b  

^a SAARLAND UNIVERSITY   (Germany)

^b NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

Author keywords

Reversible dissociation; V1V0 ATPase; Vacuolar type ATPase; Vma5p nucleotide binding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEIN SUBUNIT;

CELL MEMBRANE; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; DISSOCIATION; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; PROTON TRANSPORT;

ADENOSINE TRIPHOSPHATE; MODELS, MOLECULAR; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; VACUOLAR PROTON-TRANSLOCATING ATPASES;

EUKARYOTA;

EID: 23844516391     PISSN: 03005127     EISSN: None     Source Type: Journal    
DOI: 10.1042/BST0330883     Document Type: Conference Paper

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