2j9p
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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, penicillin-recognizing enzymes. The soaking of PBP4a in a solution of, d-alpha-aminopymelyl-epsilon-d-alanyl-d-alanine resulted in an adduct, between PBP4a and a d-alpha-aminopimelyl-epsilon-d-alanine dipeptide and, an unbound d-alanine, i.e. the products of acylation of PBP4a by, d-alpha-aminopymelyl-epsilon-d-alanyl-d-alanine with the release of a, d-alanine. The adduct also reveals a binding pocket specific to the, diaminopimelic acid, the third residue of the peptidoglycan stem, pentapeptide of B. subtilis. This pocket is specific for this class of, PBPs.
About this StructureAbout this Structure
2J9P is a Single protein structure of sequence from [1] with REZ as ligand. Known structural/functional Site: . 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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