2j9p: Difference between revisions
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Revision as of 18:23, 30 October 2007
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CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS PBP4A, AND ITS COMPLEX WITH A PEPTIDOGLYCAN MIMETIC PEPTIDE.
OverviewOverview
The genome of Bacillus subtilis encodes 16 penicillin-binding proteins, (PBPs) involved in the synthesis and/or remodelling of the peptidoglycan, during the complex life cycle of this sporulating Gram-positive rod-shaped, bacterium. PBP4a (encoded by the dacC gene) is a low-molecular mass PBP, clearly exhibiting in vitrodd-carboxypeptidase activity. We have solved, the crystal structure of this protein alone and in complex with a peptide, (d-alpha-aminopymelyl-epsilon-d-alanyl-d-alanine) that mimics the, C-terminal end of the Bacillus peptidoglycan stem peptide. PBP4a is, composed of three domains: the penicillin-binding domain with a fold, similar to the class A beta-lactamase structure and two domains inserted, between the conserved motifs 1 and 2 characteristic of the, ... [(full description)]
About this StructureAbout this Structure
2J9P is a [Single protein] structure of sequence from [[1]] with REZ as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal Structure of the Bacillus subtilis Penicillin-binding Protein 4a, and its Complex with a Peptidoglycan Mimetic Peptide., Sauvage E, Duez C, Herman R, Kerff F, Petrella S, Anderson JW, Adediran SA, Pratt RF, Frere JM, Charlier P, J Mol Biol. 2007 Aug 10;371(2):528-39. Epub 2007 Jun 2. PMID:17582436
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