ArticleThe Journal of biological chemistry2005
Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism.
Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Functional mapping and engineering of the Sec translocon unlocked by a cell-free system.Science advances · 2026Article
- The Structure ofInternational journal of molecular sciences · 2020Article
- Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis.Science advances · 2018Article
- Mutations in the Escherichia coli ribosomal protein L22 selectively suppress the expression of a secreted bacterial virulence factor.Journal of bacteriology · 2013Article
- ATPase active-site electrostatic interactions control the global conformation of the 100 kDa SecA translocase.Journal of the American Chemical Society · 2013Article
- Crystal structure of the dopamine N-acetyltransferase-acetyl-CoA complex provides insights into the catalytic mechanism.The Biochemical journal · 2012Article
- Characterization of the Escherichia coli SecA signal peptide-binding site.Journal of bacteriology · 2012Article
- Characterization of Streptococcus gordonii SecA2 as a paralogue of SecA.Journal of bacteriology · 2009Article
- Energy transduction in protein transport and the ATP hydrolytic cycle of SecA.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- ATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance for SecA2 function in macrophages.Journal of bacteriology · 2008Article
- Role of divalent metal cations in ATP hydrolysis catalyzed by the hepatitis C virus NS3 helicase: magnesium provides a bridge for ATP to fuel unwinding.Journal of molecular biology · 2007Article
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5 authors at 1 institution in 1 country.
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Abstract
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 glutamate 210 to aspartate results in a 90-fold reduction of the ATP hydrolysis rate compared with wild type SecA, 0.3 s(-1) versus 27 s(-1), respectively. SecA-E210D also releases ADP at a slower rate compared with wild type SecA, suggesting that in addition to serving as the catalytic base, glutamate 210 might aid turnover as well. Our results contradict an earlier report that proposed aspartate 133 as the catalytic base (Sato, K., Mori, H., Yoshida, M., and Mizushima, S. (1996) J. Biol. Chem. 271, 17439-17444). Re-evaluation of the SecA-D133N mutant used in that study confirms its loss of ATPase and membrane translocation activities, but surprisingly, the analogous SecA-D133A mutant retains full activity, revealing that this residue does not play a key role in catalysis.
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