ArticleJournal of structural and functional genomics2005
Crystal structures of a phosphotransacetylase from Bacillus subtilis and its complex with acetyl phosphate.
Article in Journal of structural and functional genomics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
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- Crystal structure of methanogen MtxX (Methanogen Marker Protein MMP4) fromFEMS microbes · 2026Article
- Identification of phytochemical inhibitors targeting phosphate acetyltransferase of Mycoplasma genitalium: insights from virtual screening and molecular dynamics studies.Molecular diversity · 2024Article
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- Metabolic and Structural Insights into Hydrogen Sulfide Mis-Regulation inAntioxidants (Basel, Switzerland) · 2022Article
- Crystal Structure and Molecular Mechanism of Phosphotransbutyrylase fromJournal of microbiology and biotechnology · 2021Article
- Rational Proteomic Analysis of a New DomesticatedFrontiers in microbiology · 2021Article
- Establishing an innovative carbohydrate metabolic pathway for efficient production of 2-keto-L-gulonic acid in Ketogulonicigenium robustum initiated by intronic promoters.Microbial cell factories · 2018Article
- Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation.PloS one · 2014Article
- Characterization of Clostridium thermocellum strains with disrupted fermentation end-product pathways.Journal of industrial microbiology & biotechnology · 2013Article
- Cloning, characterization and transcriptional analysis of two phosphate acetyltransferase isoforms from Azotobacter vinelandii.Molecular biology reports · 2011Article
- On the combination of molecular replacement and single-wavelength anomalous diffraction phasing for automated structure determination.Acta crystallographica. Section D, Biological crystallography · 2009Article
- Structure and function of enzymes involved in the anaerobic degradation of L-threonine to propionate.Journal of biosciences · 2007Review
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Phosphotransacetylase (Pta) [EC 2.3.1.8] plays a major role in acetate metabolism by catalyzing the reversible transfer of the acetyl group between coenzyme A (CoA) and orthophosphate: CH(3)COSCoA+HPO(4)(2-)<-->CH(3)COOPO(3)(2-) +CoASH. In this study, we report the crystal structures of Pta from Bacillus subtilis at 2.75 A resolution and its complex with acetyl phosphate, one of its substrates, at 2.85 A resolution. In addition, the Pta activity of the enzyme has been assayed. The enzyme folds into an alpha/beta architecture with two domains separated by a prominent cleft, very similar to two other known Pta structures. The enzyme-acetyl phosphate complex structure reveals a few potential substrate binding sites. Two of them are located in the middle of the interdomain cleft: each one is surrounded by a region of strictly and highly conserved residues. High structural similarities are found with 4-hydroxythreonine-4-phosphate dehydrogenase (PdxA), and isocitrate and isopropylmalate dehydrogenases, all of which utilize NADP+ as their cofactor, which binds in the interdomain cleft. Their substrate binding sites are close to the acetyl phosphate binding sites of Pta in the cleft as well. These results suggest that the CoA is likely to bind to the interdomain cleft of Pta in a similar way as NADP+ binds to the other three enzymes.
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