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| | <StructureSection load='1gce' size='340' side='right'caption='[[1gce]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1gce' size='340' side='right'caption='[[1gce]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gce]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aerobacter_cloacae"_(jordan_1890)_bergey_et_al._1923 "aerobacter cloacae" (jordan 1890) bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GCE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gce]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GCE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2blt|2blt]]</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]] 1.8Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=1gce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gce OCA], [https://pdbe.org/1gce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gce RCSB], [https://www.ebi.ac.uk/pdbsum/1gce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gce ProSAT]</span></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=1gce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gce OCA], [http://pdbe.org/1gce PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gce RCSB], [http://www.ebi.ac.uk/pdbsum/1gce PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gce ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AMPC_ENTCL AMPC_ENTCL]] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. | + | [https://www.uniprot.org/uniprot/AMPC_ENTCL AMPC_ENTCL] 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: Enterobacter cloacae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Crichlow, G V]] | + | [[Category: Crichlow GV]] |
| - | [[Category: Knox, J R]] | + | [[Category: Knox JR]] |
| - | [[Category: Kuzin, A P]] | + | [[Category: Kuzin AP]] |
| - | [[Category: Nukaga, M]] | + | [[Category: Nukaga M]] |
| - | [[Category: Sawai, T]] | + | [[Category: Sawai T]] |
| - | [[Category: Beta-lactam hydrolase]]
| + | |
| - | [[Category: Cephalosporinase]]
| + | |
| - | [[Category: Drug design]]
| + | |
| - | [[Category: Extended-spectrum beta- lactamase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
AMPC_ENTCL 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
A class C beta-lactamase from a clinical isolate of Enterobacter cloacae strain GC1 with improved hydrolytic activity for oxyimino beta-lactam antibiotics has been analyzed by X-ray crystallography to 1.8 A resolution. Relative to the wild-type P99 beta-lactamase, this natural mutant contains a highly unique tandem repeat Ala211-Val212-Arg213 [Nugaka et al. (1995) J. Biol. Chem. 270, 5729-5735]. The 39.4 kDa chromosomal beta-lactamase crystallizes from poly(ethylene glycol) 8000 in potassium phosphate in space group P2(1)2(1)2 with cell dimensions a = 78.0 A, b = 69.5 A, and c = 63.1 A. The crystal structure was solved by the molecular replacement method, and the model has been refined to an R-factor of 0.20 for all nonzero data from 8 to 1.8 A. Deviations of model bonds and angles from ideal values are 0.008 A and 1.4 degrees, respectively. Overlay of alpha-carbon atoms in the GC1 and P99 beta-lactamases results in an rms deviation of 0.6 A. Largest deviations occur in a loop containing Gln120 and in the Omega loop region (200-218) where the three residues 213-215 are disordered. Possibly as a result of this disorder, the width of the opening to the substrate binding cavity, as measured from the 318-324 beta-strand to two loops containing Gln120 and Tyr150 on the other side, is 0.6-1.4 A wider than in P99. It is suggested that conformational flexibility in the expanded Omega loop, and its influence on adjacent protein structure, may facilitate hydrolysis of oxyimino beta-lactams by making the acyl intermediate more open to attack by water. Nevertheless, backbone atoms in core catalytic site residues Ser64, Lys67, Tyr150, Asn152, Lys318, and Ser321 deviate only 0.4 A (rmsd) from atoms in P99. A rotation of a potential catalytic base, Tyr150, relative to P99 at pH 8, is consistent with the requirement for a lower than normal pK(a) for this residue.
Structure of the extended-spectrum class C beta-lactamase of Enterobacter cloacae GC1, a natural mutant with a tandem tripeptide insertion.,Crichlow GV, Kuzin AP, Nukaga M, Mayama K, Sawai T, Knox JR Biochemistry. 1999 Aug 10;38(32):10256-61. PMID:10441119[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Crichlow GV, Kuzin AP, Nukaga M, Mayama K, Sawai T, Knox JR. Structure of the extended-spectrum class C beta-lactamase of Enterobacter cloacae GC1, a natural mutant with a tandem tripeptide insertion. Biochemistry. 1999 Aug 10;38(32):10256-61. PMID:10441119 doi:10.1021/bi9908787
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