Premium
Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F 1 ‐ATPase
Author(s) -
Duncan Thomas M.,
Parsonage Derek,
Senior Alan E.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81519-8
Subject(s) - protein subunit , cyclic nucleotide binding domain , nucleotide , atpase , escherichia coli , domain (mathematical analysis) , nucleic acid sequence , binding domain , peptide sequence , protein tertiary structure , binding site , biochemistry , sequence (biology) , chemistry , biology , enzyme , gene , mathematical analysis , mathematics
We propose a working model for the tertiary structure of the nucleotide‐binding domain of the β‐subunit of E. coli F 1 ‐ATPase, derived from secondary structure prediction and from comparison of the amino acid sequence with the sequences of other nucleotide‐binding proteins of known three‐dimensional structure. The model is consistent with previously published results of specific chemical modification studies and of analyses of mutations in the β‐subunit and its implications for subunit interactions and catalytic mechanism in F 1 ‐ATPases are discussed.