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Article

Steric limitations in the interaction of the ATP binding domains of the ArsA ATPase.

The Journal of biological chemistry - 20 Mar 1998

Li J, Rosen B P

Abstract excerpt

ArsA, the catalytic subunit of an anion-translocating ATPase, has two consensus nucleotide binding sites, one N-terminal and one C-terminal. A mutation producing a G15C substitution in the N-terminal domain resulted in substantial reductions in arsenite resistance, transport, and ATPase activity. A second site revertant (A344V) adjacent to the C-terminal nucleotide binding site was previously shown to restore...

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Identifiers

PMID: 9506981
DOI: 10.1074/jbc.273.12.6796

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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