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| | <StructureSection load='1k07' size='340' side='right'caption='[[1k07]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='1k07' size='340' side='right'caption='[[1k07]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1k07]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33297 Atcc 33297]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K07 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1K07 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1k07]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fluoribacter_gormanii Fluoribacter gormanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K07 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jt1|1jt1]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaFEZ-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=464 ATCC 33297])</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=1k07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k07 OCA], [https://pdbe.org/1k07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k07 RCSB], [https://www.ebi.ac.uk/pdbsum/1k07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k07 ProSAT]</span></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> | + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1k07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k07 OCA], [http://pdbe.org/1k07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k07 RCSB], [http://www.ebi.ac.uk/pdbsum/1k07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k07 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9K578_9GAMM Q9K578_9GAMM] |
| | == 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: Atcc 33297]] | + | [[Category: Fluoribacter gormanii]] |
| - | [[Category: Beta-lactamase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dideberg, O]] | + | [[Category: Dideberg O]] |
| - | [[Category: Frere, J M]] | + | [[Category: Frere JM]] |
| - | [[Category: Galleni, M]] | + | [[Category: Galleni M]] |
| - | [[Category: Garcia-Saez, I]] | + | [[Category: Garcia-Saez I]] |
| - | [[Category: Kahn, R]] | + | [[Category: Kahn R]] |
| - | [[Category: Mercuri, P S]] | + | [[Category: Mercuri PS]] |
| - | [[Category: Papamicael, C]] | + | [[Category: Papamicael C]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Monomer with alpha-beta/beta-alpha fold. two monomers per assymmetric unit]]
| + | |
| Structural highlights
Function
Q9K578_9GAMM
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
The beta-lactamases are involved in bacterial resistance to penicillin and related compounds. Members of the metallo-enzyme class are now found in many pathogenic bacteria and are thus becoming of major clinical importance. The structures of the Zn-beta-lactamase from Fluoribacter gormanii (FEZ-1) in the native and in the complex form are reported here. FEZ-1 is a monomeric enzyme, which possesses two zinc-binding sites. These structures are discussed in comparison with those of the tetrameric L1 enzyme produced by Stenotrophomonas maltophilia. From this analysis, amino acids involved in the oligomerization of L1 are clearly identified. Despite the similarity in fold, the active site of FEZ-1 was found to be significantly different. Two residues, which were previously implicated in function, are not present in L1 or in FEZ-1. The broad-spectrum substrate profile of Zn-beta-lactamases arises from the rather wide active-site cleft, where various beta-lactam compounds can be accommodated.
Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril.,Garcia-Saez I, Mercuri PS, Papamicael C, Kahn R, Frere JM, Galleni M, Rossolini GM, Dideberg O J Mol Biol. 2003 Jan 24;325(4):651-60. PMID:12507470[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Garcia-Saez I, Mercuri PS, Papamicael C, Kahn R, Frere JM, Galleni M, Rossolini GM, Dideberg O. Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril. J Mol Biol. 2003 Jan 24;325(4):651-60. PMID:12507470
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