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Structure paper

TitleStructures of the Michaelis Complex (1.2 A) and the Covalent Acyl Intermediate (2.0 A) of Cefamandole Bound in the Active Sites of the Mycobacterium tuberculosis beta-Lactamase K73A and E166A Mutants.
Journal, issue, pagesBiochemistry, Vol. 49, Page 9685-9687, Year 2010
Publish dateMay 28, 2010 (structure data deposition date)
AuthorsTremblay, L.W. / Xu, H. / Blanchard, J.S.
External linksBiochemistry / PubMed:20961112
MethodsX-ray diffraction
Resolution1.22 - 2 Å
Structure data

PDB-3n8s:
Crystal Structure of BlaC-E166A covalently bound with Cefamandole
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3ny4:
Crystal Structure of BlaC-K73A bound with Cefamandole
Method: X-RAY DIFFRACTION / Resolution: 1.22 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-XD2:
(2R)-2-[(1R)-1-{[(2R)-2-hydroxy-2-phenylacetyl]amino}-2-oxoethyl]-5-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid / antibiotic*YM

ChemComp-HOH:
WATER

ChemComp-SMX:
(6R,7R)-7-{[(2R)-2-hydroxy-2-phenylacetyl]amino}-3-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid / antibiotic*YM

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsHYDROLASE/ANTIBIOTIC / penicillin binding protein / beta-lactam covalent adduct / HYDROLASE-ANTIBIOTIC complex / beta-lactam complex

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