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Structure paper

TitleStructure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions.
Journal, issue, pagesNat Commun, Vol. 10, Page 3868-3868, Year 2019
Publish dateApr 11, 2019 (structure data deposition date)
AuthorsPatel, K.D. / d'Andrea, F.B. / Gaudelli, N.M. / Buller, A.R. / Townsend, C.A. / Gulick, A.M.
External linksNat Commun / PubMed:31455765
MethodsX-ray diffraction
Resolution1.94 - 1.99 Å
Structure data

PDB-6ojc:
A high-resolution crystal structure of NocB thioesterase domain from Nocardicin cluster
Method: X-RAY DIFFRACTION / Resolution: 1.94 Å

PDB-6ojd:
A high-resolution crystal structure of covalent complex of NocB thioesterase domain with fluorophosphonate nocardicin G analog
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-MUY:
(R)-[(S)-[(3S)-3-{[(2R)-2-amino-2-(4-hydroxyphenyl)acetyl]amino}-2-oxoazetidin-1-yl](4-hydroxyphenyl)methyl]methylphosphinic acid

ChemComp-CA:
Unknown entry

Source
  • nocardia uniformis subsp. tsuyamanensis (bacteria)
KeywordsHYDROLASE / Nonribosomal peptide synthetase (NRPS) / thioesterase / epimerization / alpha/beta hydrolase fold

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