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| | <StructureSection load='2bg1' size='340' side='right'caption='[[2bg1]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2bg1' size='340' side='right'caption='[[2bg1]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bg1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strr6 Strr6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BG1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bg1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BG1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bg1 OCA], [http://pdbe.org/2bg1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bg1 RCSB], [http://www.ebi.ac.uk/pdbsum/2bg1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bg1 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bg1 OCA], [https://pdbe.org/2bg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bg1 RCSB], [https://www.ebi.ac.uk/pdbsum/2bg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bg1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7CRA4_STRR6 Q7CRA4_STRR6] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Penicillin-binding protein|Penicillin-binding protein]] | + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidoglycan glycosyltransferase]] | + | [[Category: Streptococcus pneumoniae R6]] |
| - | [[Category: Strr6]] | + | [[Category: Dessen A]] |
| - | [[Category: Dessen, A]] | + | [[Category: Di Guilmi AM]] |
| - | [[Category: Dideberg, O]] | + | [[Category: Dideberg O]] |
| - | [[Category: Guilmi, A M.Di]]
| + | [[Category: Job V]] |
| - | [[Category: Job, V]] | + | [[Category: Macheboeuf P]] |
| - | [[Category: Macheboeuf, P]] | + | [[Category: Vernet T]] |
| - | [[Category: Vernet, T]] | + | |
| - | [[Category: Cell wall]]
| + | |
| - | [[Category: Peptidoglycan]]
| + | |
| - | [[Category: Peptidoglycan synthesis multifunctional enzyme]]
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| Structural highlights
Function
Q7CRA4_STRR6
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Macheboeuf P, Di Guilmi AM, Job V, Vernet T, Dideberg O, Dessen A. Active site restructuring regulates ligand recognition in class A penicillin-binding proteins. Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):577-82. Epub 2005 Jan 6. PMID:15637155
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