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Structure paper

TitleAutoproteolytic Activation of ThnT Results in Structural Reorganization Necessary for Substrate Binding and Catalysis.
Journal, issue, pagesJ. Mol. Biol., Vol. 422, Page 508-518, Year 2012
Publish dateAug 30, 2011 (structure data deposition date)
AuthorsBuller, A.R. / Labonte, J.W. / Freeman, M.F. / Wright, N.T. / Schildbach, J.F. / Townsend, C.A.
External linksJ. Mol. Biol. / PubMed:22706025
MethodsX-ray diffraction
Resolution1.8 - 2 Å
Structure data

PDB-3tm1:
Crystal structure of mature ThnT, a pantetheine hydrolase
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3tm2:
Crystal structure of mature ThnT with a covalently bound product mimic
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-TXI:
(2R)-N-(4-chloro-3-oxobutyl)-2,4-dihydroxy-3,3-dimethylbutanamide

Source
  • streptomyces cattleya (bacteria)
KeywordsHYDROLASE / DOM-fold / amidohydrolase / autoproteolytic / carbapenem / DmpA/OAT superfamily / Pantetheine hydrolase / thienamcyin biosynthesis / HYDROLASE/HYDROLASE INHIBITOR / pantetheine / inhibitor / thienamycin biosynthesis / O-(2-oxo-4-pantoamindobutyl)threonine / HYDROLASE-HYDROLASE INHIBITOR complex

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