2j9p: Difference between revisions

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.

2J9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with REZ as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J9P OCA].  

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