A MODEL FOR THE CATALYTIC SITE OF F1-ATPASE BASED ON ANALOGIES TO NUCLEOTIDE-BINDING DOMAINS OF KNOWN STRUCTURE

被引:29
作者
DUNCAN, TM
CROSS, RL
机构
[1] Department of Biochemistry and Molecular Biology, SUNY Health Science Center at Syracuse, Syracuse, 13210, New York
关键词
F1-ATPASE; NUCLEOTIDE BINDING SITES; PROTEIN FOLDING; STRUCTURE PREDICTION;
D O I
10.1007/BF00762362
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
An updated topological model is constructed for the catalytic nucleotide-binding site of the F1-ATPase. The model is based on analogies to the known structures of the MgATP site on adenylate kinase and the guanine nucleotide sites on elongation factor Tu (Ef-Tu) and the ras p21 protein. Recent studies of these known nucleotide-binding domains have revealed several common functional features and similar alignment of nucleotide in their binding folds, and these are used as a framework for evaluating results of affinity labeling and mutagenesis studies of the beta subunit of F1. Several potentially important residues on beta are noted that have not yet been studied by mutagenesis or affinity labeling.
引用
收藏
页码:453 / 461
页数:9
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