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Structure paper

TitleCatalytic mechanism of the Streptomyces K15 DD-transpeptidase/penicillin-binding protein probed by site-directed mutagenesis and structural analysis.
Journal, issue, pagesBiochemistry, Vol. 42, Page 2895-2906, Year 2003
Publish dateApr 7, 2000 (structure data deposition date)
AuthorsRhazi, N. / Charlier, P. / Dehareng, D. / Engher, D. / Vermeire, M. / Frere, J.M. / Nguyen-Disteche, M. / Fonze, E.
External linksBiochemistry / PubMed:12627955
MethodsX-ray diffraction
Resolution1.55 - 2.2 Å
Structure data

PDB-1es2:
S96A mutant of streptomyces K15 DD-transpeptidase
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-1es3:
C98A mutant of streptomyces K15 DD-transpeptidase
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1es4:
C98N mutant of streptomyces K15 DD-transpeptidase
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1j9m:
K38H mutant of Streptomyces K15 DD-transpeptidase
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

Source
  • streptomyces sp. (bacteria)
KeywordsHYDROLASE / PENICILLIN-BINDING / DD-TRANSPEPTIDASE / SERINE PEPTIDASE / BETA-LACTAMASE / HYDROLASE CARBOXYPEPTIDASE

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