2bg1
From Proteopedia
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| - | [[Image:2bg1.gif|left|200px]] | + | [[Image:2bg1.gif|left|200px]] |
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| - | '''ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA PENICILLIN-BINDING PROTEINS (PBPS)''' | + | {{Structure |
| + | |PDB= 2bg1 |SIZE=350|CAPTION= <scene name='initialview01'>2bg1</scene>, resolution 1.9Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptidoglycan_glycosyltransferase Peptidoglycan glycosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.129 2.4.1.129] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ACTIVE SITE RESTRUCTURING REGULATES LIGAND RECOGNITION IN CLASSA PENICILLIN-BINDING PROTEINS (PBPS)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BG1 is a [ | + | 2BG1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BG1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15637155 15637155] |
[[Category: Peptidoglycan glycosyltransferase]] | [[Category: Peptidoglycan glycosyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: peptidoglycan synthesis multifunctional enzyme]] | [[Category: peptidoglycan synthesis multifunctional enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:01:28 2008'' |
Revision as of 14:01, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Peptidoglycan glycosyltransferase, with EC number 2.4.1.129 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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.
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
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