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| | <StructureSection load='1ga0' size='340' side='right'caption='[[1ga0]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='1ga0' size='340' side='right'caption='[[1ga0]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ga0]] 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=1GA0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1GA0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ga0]] 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=1GA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GA0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DVR:3-(4-CARBAMOYL-1-CARBOXY-2-METHYLSULFONYL-BUTA-1,3-DIENYLAMINO)-INDOLIZINE-2-CARBOXYLIC+ACID'>DVR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gce|1gce]], [[1bls|1bls]], [[2blt|2blt]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DVR:3-(4-CARBAMOYL-1-CARBOXY-2-METHYLSULFONYL-BUTA-1,3-DIENYLAMINO)-INDOLIZINE-2-CARBOXYLIC+ACID'>DVR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=550 "Aerobacter cloacae" (Jordan 1890) Bergey et al. 1923])</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=1ga0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ga0 OCA], [https://pdbe.org/1ga0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ga0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ga0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ga0 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=1ga0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ga0 OCA], [http://pdbe.org/1ga0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ga0 RCSB], [http://www.ebi.ac.uk/pdbsum/1ga0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ga0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q59401_ENTCL Q59401_ENTCL] |
| | == 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: Buynak, J D]] | + | [[Category: Buynak JD]] |
| - | [[Category: Crichlow, G V]] | + | [[Category: Crichlow GV]] |
| - | [[Category: Knox, J R]] | + | [[Category: Knox JR]] |
| - | [[Category: Nukaga, M]] | + | [[Category: Nukaga M]] |
| - | [[Category: Cephalosporinase]]
| + | |
| - | [[Category: Class c beta-lactamase]]
| + | |
| - | [[Category: Conformational change]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inhibition]]
| + | |
| - | [[Category: Mixed alpha/beta]]
| + | |
| Structural highlights
Function
Q59401_ENTCL
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 crystallographic structure of the Enterobacter cloacae GC1 extended-spectrum class C beta-lactamase, inhibited by a new 7-alkylidenecephalosporin sulfone, has been determined by X-ray diffraction at 100 K to a resolution of 1.6 A. The crystal structure was solved by molecular replacement using the unliganded structure [Crichlow et al. (1999) Biochemistry 38, 10256-10261] and refined to a crystallographic R-factor equal to 0.183 (R(free) 0.208). Cryoquenching of the reaction of the sulfone with the enzyme produced an intermediate that is covalently bound via Ser64. After acylation of the beta-lactam ring, the dihydrothiazine dioxide ring opened with departure of the sulfinate. Nucleophilic attack of a side chain pyridine nitrogen atom on the C6 atom of the resultant imine yielded a bicyclic aromatic system which helps to stabilize the acyl enzyme to hydrolysis. A structural assist to this resonance stabilization is the positioning of the anionic sulfinate group between the probable catalytic base (Tyr150) and the acyl ester bond so as to block the approach of a potentially deacylating water molecule. Comparison of the liganded and unliganded protein structures showed that a major movement (up to 7 A) and refolding of part of the Omega-loop (215-224) accompanies the binding of the inhibitor. This conformational flexibility in the Omega-loop may form the basis of an extended-spectrum activity of class C beta-lactamases against modern cephalosporins.
Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone.,Crichlow GV, Nukaga M, Doppalapudi VR, Buynak JD, Knox JR Biochemistry. 2001 May 29;40(21):6233-9. PMID:11371184[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Crichlow GV, Nukaga M, Doppalapudi VR, Buynak JD, Knox JR. Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone. Biochemistry. 2001 May 29;40(21):6233-9. PMID:11371184
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