1w79
From Proteopedia
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CRYSTAL STRUCTURE OF THE DD-TRANSPEPTIDASE-CARBOXYPEPTIDASE FROM ACTINOMADURA R39
Overview
Actinomadura sp. R39 produces an exocellular, DD-peptidase/penicillin-binding protein (PBP) whose primary structure is, similar to that of Escherichia coli PBP4. It is characterized by a high, beta-lactam-binding activity (second order rate constant for the acylation, of the active site serine by benzylpenicillin: k2/K = 300 mm(-1) s(-1))., The crystal structure of the DD-peptidase from Actinomadura R39 was solved, at a resolution of 1.8 angstroms by single anomalous dispersion at the, cobalt resonance wavelength. The structure is composed of three domains: a, penicillin-binding domain similar to the penicillin-binding domain of E., coli PBP5 and two domains of unknown function. In most multimodular PBPs, additional domains are generally located at the C or N termini of the, penicillin-binding domain. In R39, the other two domains are inserted in, the penicillin-binding domain, between the SXXK and SXN motifs, in a, manner similar to "Matryoshka dolls." One of these domains is composed of, a five-stranded beta-sheet with two helices on one side, and the other, domain is a double three-stranded beta-sheet inserted in the previous, domain. Additionally, the 2.4-angstroms structure of the acyl-enzyme, complex of R39 with nitrocefin reveals the absence of active site, conformational change upon binding the beta-lactams.
About this Structure
1W79 is a Single protein structure of sequence from [1] with SO4 and MG as ligands. Active as Serine-type D-Ala-D-Ala carboxypeptidase, with EC number 3.4.16.4 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins., Sauvage E, Herman R, Petrella S, Duez C, Bouillenne F, Frere JM, Charlier P, J Biol Chem. 2005 Sep 2;280(35):31249-56. Epub 2005 Jun 29. PMID:15987687
Page seeded by OCA on Mon Nov 5 15:23:39 2007
