2bg1
From Proteopedia
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ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA PENICILLIN-BINDING PROTEINS (PBPS)
Overview
Bacterial cell division is a complex, multimolecular process that requires, biosynthesis of new peptidoglycan by penicillin-binding proteins (PBPs), during cell wall elongation and septum formation steps. Streptococcus, pneumoniae has three bifunctional (class A) PBPs that catalyze both, polymerization of glycan chains (glycosyltransfer) and cross-linking of, pentapeptidic bridges (transpeptidation) during the peptidoglycan, biosynthetic process. In addition to playing important roles in cell, division, PBPs are also the targets for beta-lactam antibiotics and thus, play key roles in drug-resistance mechanisms. The crystal structure of a, soluble form of pneumococcal PBP1b (PBP1b*) has been solved to 1.9 A, thus, providing previously undescribed structural information regarding a class, A ... [(full description)]
About this Structure
2BG1 is a [Single protein] structure of sequence from [Streptococcus pneumoniae] with SO4 and CL as [ligands]. Active as [[1]], with EC number [2.4.1.129]. Full crystallographic information is available from [OCA].
Reference
Active site restructuring regulates ligand recognition in class A penicillin-binding proteins., Macheboeuf P, Di Guilmi AM, Job V, Vernet T, Dideberg O, Dessen A, Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):577-82. Epub 2005 Jan 6. PMID:15637155
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