1w8y

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spinqualitylabelsall models 1w8y, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE NITROCEFIN ACYL-DD-PEPTIDASE 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, ... [(full description)]

About this Structure

1W8Y is a [Single protein] structure of sequence from [Actinomadura] with SO4, MG and NCF as [ligands]. Active as [[1]], with EC number [3.4.16.4]. 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

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