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Crystal structures of a phosphotransacetylase from Bacillus subtilis and its complex with acetyl phosphate.

Xu QS, Jancarik J, Lou Y, Kuznetsova K, Yakunin AF, Yokota H, Adams P, Kim R, Kim SH
J Struct Funct Genomics 6 269-79 (2005)
Cited: 16 times
EuropePMC logo PMID: 16283428

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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  4. Biophysical and biochemical studies support TP0094 as a phosphotransacetylase in an acetogenic energy-conservation pathway in Treponema pallidum. Brautigam CA, Deka RK, Tso SC, Liu WZ, Norgard MV. PLoS One 18 e0283952 (2023)


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  2. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Lu YJ, Zhang YM, Grimes KD, Qi J, Lee RE, Rock CO. Mol Cell 23 765-772 (2006)
  3. Characterization of Clostridium thermocellum strains with disrupted fermentation end-product pathways. van der Veen D, Lo J, Brown SD, Johnson CM, Tschaplinski TJ, Martin M, Engle NL, van den Berg RA, Argyros AD, Caiazza NC, Guss AM, Lynd LR. J Ind Microbiol Biotechnol 40 725-734 (2013)
  4. Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation. Campos-Bermudez VA, Bologna FP, Andreo CS, Drincovich MF. FEBS J 277 1957-1966 (2010)
  5. Cloning, characterization and transcriptional analysis of two phosphate acetyltransferase isoforms from Azotobacter vinelandii. Dimou M, Venieraki A, Liakopoulos G, Katinakis P. Mol Biol Rep 38 3653-3663 (2011)
  6. Establishing an innovative carbohydrate metabolic pathway for efficient production of 2-keto-L-gulonic acid in Ketogulonicigenium robustum initiated by intronic promoters. Wang CY, Li Y, Gao ZW, Liu LC, Zhang MY, Zhang TY, Wu CF, Zhang YX. Microb Cell Fact 17 81 (2018)
  7. Extensive regulation of enzyme activity by phosphorylation in Escherichia coli. Schastnaya E, Raguz Nakic Z, Gruber CH, Doubleday PF, Krishnan A, Johns NI, Park J, Wang HH, Sauer U. Nat Commun 12 5650 (2021)
  8. Rational Proteomic Analysis of a New Domesticated Klebsiella pneumoniae x546 Producing 1,3-Propanediol. Wang X, Zhang L, Chen H, Wang P, Yin Y, Jin J, Xu J, Wen J. Front Microbiol 12 770109 (2021)
  9. Metabolic and Structural Insights into Hydrogen Sulfide Mis-Regulation in Enterococcus faecalis. Walsh BJC, Costa SS, Edmonds KA, Trinidad JC, Issoglio FM, Brito JA, Giedroc DP. Antioxidants (Basel) 11 1607 (2022)
  10. Crystal Structure and Molecular Mechanism of Phosphotransbutyrylase from Clostridium acetobutylicum. Kim S, Kim KJ. J Microbiol Biotechnol 31 1393-1400 (2021)
  11. Identification of phytochemical inhibitors targeting phosphate acetyltransferase of Mycoplasma genitalium: insights from virtual screening and molecular dynamics studies. Barik K, Arya PK, Singh AK, Kumar A. Mol Divers (2023)


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