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TitleBiophysical and biochemical studies support TP0094 as a phosphotransacetylase in an acetogenic energy-conservation pathway in Treponema pallidum.
Journal, issue, pagesPlos One, Vol. 18, Page e0283952-e0283952, Year 2023
Publish dateDec 16, 2022 (structure data deposition date)
AuthorsBrautigam, C.A. / Deka, R.K. / Tso, S.C. / Liu, W.Z. / Norgard, M.V.
External linksPlos One / PubMed:37200262
MethodsX-ray diffraction
Resolution1.95 Å
Structure data

PDB-8fir:
Crystal structure of TpPta, a phosphotransacetylase from Treponema pallidum
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CIT:
CITRIC ACID

ChemComp-HOH:
WATER

Source
  • treponema pallidum (bacteria)
KeywordsTRANSFERASE / phosphotransacetylase / syphilis / T. pallidum / metabolic enzyme

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