Mutational analysis of arginine 177 in the nucleotide binding site of beta-actin.

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Article

Mutational analysis of arginine 177 in the nucleotide binding site of beta-actin.

European journal of biochemistry - 1 Jul 2000

Schüler H, Nyåkern M, Schutt C E, Lindberg U, Karlsson R

Abstract excerpt

Actin ADP-ribosylated at arginine 177 is unable to hydrolyze ATP, and the R177 side chain is in a position similar to that of the catalytically essential lysine 71 in heat shock cognate protein Hsc70, another member of the actin-fold family of proteins. Therefore, actin residue R177 has been implicated in the mechanism of ATP hydrolysis. This paper compares wild-type beta-actin with a mutant in which R177 has...

Topics

Actins
Adenosine Triphosphatases
Adenosine Triphosphate
Arginine
Binding Sites
Hot Temperature
Microscopy, Fluorescence
Mutation
Phalloidine

Source

Open in PubMed

Identifiers

PMID: 10866806

Provenance

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