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| - | [[Image:2bg1.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2bg1| PDB=2bg1 | SCENE= }} | | {{STRUCTURE_2bg1| PDB=2bg1 | SCENE= }} |
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| - | '''ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA PENICILLIN-BINDING PROTEINS (PBPS)'''
| + | ===ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA PENICILLIN-BINDING PROTEINS (PBPS)=== |
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| - | ==Overview==
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| - | 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 PBP from any organism. PBP1b* is a three-domain molecule harboring a short peptide from the glycosyltransferase domain bound to an interdomain linker region, the transpeptidase domain, and a C-terminal region. The structure of PBP1b* complexed with beta-lactam antibiotics reveals that ligand recognition requires a conformational modification involving conserved elements within the cleft. The open and closed structures of PBP1b* suggest how class A PBPs may become activated as novel peptidoglycan synthesis becomes necessary during the cell division process. In addition, this structure provides an initial framework for the understanding of the role of class A PBPs in the development of antibiotic resistance.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15637155}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15637155 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15637155}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Cell wall]] | | [[Category: Cell wall]] |
| | [[Category: Peptidoglycan synthesis multifunctional enzyme]] | | [[Category: Peptidoglycan synthesis multifunctional enzyme]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:14:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:26:55 2008'' |
Revision as of 02:26, 28 July 2008
Template:STRUCTURE 2bg1
ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA PENICILLIN-BINDING PROTEINS (PBPS)
Template:ABSTRACT PUBMED 15637155
About this Structure
2BG1 is a Single protein structure of sequence from Streptococcus pneumoniae. 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
Page seeded by OCA on Mon Jul 28 05:26:55 2008
