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Article

Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism.

The Journal of biological chemistry - 15 Apr 2005

Zito Christopher R, Antony Edwin, Hunt John F, Oliver Donald B, Hingorani Manju M

Abstract excerpt

Escherichia coli SecA uses ATP to drive the transport of proteins across cell membranes. Glutamate 210 in the "DEVD" Walker B motif of the SecA ATP-binding site has been proposed as the catalytic base for ATP hydrolysis (Hunt, J. F., Weinkauf, S., Henry, L., Fak, J. J., McNicholas, P., Oliver, D. B., and Deisenhofer, J. (2002) Science 297, 2018-2026). Consistent with this hypothesis, we find that mutation of...

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Identifiers

PMID: 15710614
DOI: 10.1074/jbc.M414224200
PMCID: PMC4684309

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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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Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism.PMID 15710614Read ↗

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