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PMID: 2876918 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Structure of the nucleotide-binding domain in the beta-subunit of Escherichia coli F1-ATPase.

FEBS letters ·Vol. 208 ·No. 1 ·1986-11-10 ·Pages 1-6

Duncan TM, Parsonage D, Senior AE

Abstract

We propose a working model for the tertiary structure of the nucleotide-binding domain of the beta-subunit of E. coli F1-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 beta-subunit and its implications for subunit interactions and catalytic mechanism in F1-ATPases are discussed.

MeSH Terms
Amino Acid Sequence Binding Sites Carrier Proteins Cyclic AMP Receptor Protein Escherichia coli/enzymology Models, Molecular Protein Conformation Proton-Translocating ATPases
Chemicals
Carrier Proteins Cyclic AMP Receptor Protein Proton-Translocating ATPases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Duncan T M
Parsonage D
Senior A E
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1986-11-10
Pages
1-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NIGMS NIH HHS · GM25349 · United States
NIGMS NIH HHS · GM29805 · United States
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