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| | <StructureSection load='2qz6' size='340' side='right'caption='[[2qz6]], [[Resolution|resolution]] 2.26Å' scene=''> | | <StructureSection load='2qz6' size='340' side='right'caption='[[2qz6]], [[Resolution|resolution]] 2.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2qz6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2QZ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2qz6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QZ6 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></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]] 2.26Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2qz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qz6 OCA], [http://pdbe.org/2qz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qz6 RCSB], [http://www.ebi.ac.uk/pdbsum/2qz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qz6 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=2qz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qz6 OCA], [https://pdbe.org/2qz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qz6 RCSB], [https://www.ebi.ac.uk/pdbsum/2qz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qz6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AMPC_PSEFL AMPC_PSEFL]] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. | + | [https://www.uniprot.org/uniprot/AMPC_PSEFL AMPC_PSEFL] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-lactamase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Pseudomonas fluorescens]] | | [[Category: Pseudomonas fluorescens]] |
| - | [[Category: Charlier, P]] | + | [[Category: Charlier P]] |
| - | [[Category: Kerff, F]] | + | [[Category: Kerff F]] |
| - | [[Category: Massant, J]] | + | [[Category: Massant J]] |
| - | [[Category: Michaux, C]] | + | [[Category: Michaux C]] |
| - | [[Category: Wouters, J]] | + | [[Category: Wouters J]] |
| - | [[Category: Antibiotic resistance]]
| + | |
| - | [[Category: Class c beta-lactamase]]
| + | |
| - | [[Category: Cold adaptation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Periplasm]]
| + | |
| - | [[Category: Psychrophile]]
| + | |
| Structural highlights
Function
AMPC_PSEFL This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
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
In this study, the crystal structure of a class C beta-lactamase from a psychrophilic organism, Pseudomonas fluorescens, has been refined to 2.2 A resolution. It is one of the few solved crystal structures of psychrophilic proteins. The structure was compared with those of homologous mesophilic enzymes and of another, modeled, psychrophilic protein. The elucidation of the 3D structure of this enzyme provides additional insights into the features involved in cold adaptation. Structure comparison of the psychrophilic and mesophilic beta-lactamases shows that electrostatics seems to play a major role in low-temperature adaptation, with a lower total number of ionic interactions for cold enzymes. The psychrophilic enzymes are also characterized by a decreased number of hydrogen bonds, a lower content of prolines, and a lower percentage of arginines in comparison with lysines. All these features make the structure more flexible so that the enzyme can behave as an efficient catalyst at low temperatures.
Crystal structure of a cold-adapted class C beta-lactamase.,Michaux C, Massant J, Kerff F, Frere JM, Docquier JD, Vandenberghe I, Samyn B, Pierrard A, Feller G, Charlier P, Van Beeumen J, Wouters J FEBS J. 2008 Apr;275(8):1687-97. Epub 2008 Feb 29. PMID:18312599[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Michaux C, Massant J, Kerff F, Frere JM, Docquier JD, Vandenberghe I, Samyn B, Pierrard A, Feller G, Charlier P, Van Beeumen J, Wouters J. Crystal structure of a cold-adapted class C beta-lactamase. FEBS J. 2008 Apr;275(8):1687-97. Epub 2008 Feb 29. PMID:18312599 doi:10.1111/j.1742-4658.2008.06324.x
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