1skf
CRYSTAL STRUCTURE OF THE STREPTOMYCES K15 DD-TRANSPEPTIDASE
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OverviewOverview
The serine DD-transpeptidase/penicillin-binding protein of Streptomyces, K15 catalyzes peptide bond formation in a way that mimics the, penicillin-sensitive peptide cross-linking reaction involved in bacterial, cell wall peptidoglycan assembly. The Streptomyces K15 enzyme is peculiar, in that it can be considered as an intermediate between classical, penicillin-binding proteins, for which benzylpenicillin is a very, efficient inactivator, and the resistant penicillin-binding proteins that, have a low penicillin affinity. With its moderate penicillin sensitivity, the Streptomyces K15 DD-transpeptidase would be helpful in the, understanding of the structure-activity relationship of this, penicillin-recognizing protein superfamily. The structure of the, Streptomyces K15 enzyme has been ... [(full description)]
About this StructureAbout this Structure
1SKF is a [Single protein] structure of sequence from [Streptomyces sp.]. Active as [Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [3.4.16.4]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of a penicilloyl-serine transferase of intermediate penicillin sensitivity. The DD-transpeptidase of streptomyces K15., Fonze E, Vermeire M, Nguyen-Disteche M, Brasseur R, Charlier P, J Biol Chem. 1999 Jul 30;274(31):21853-60. PMID:10419503
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