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1ci9

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[[Image:1ci9.jpg|left|200px]]
 
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{{Structure
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==DFP-INHIBITED ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI==
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|PDB= 1ci9 |SIZE=350|CAPTION= <scene name='initialview01'>1ci9</scene>, resolution 1.800&Aring;
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<StructureSection load='1ci9' size='340' side='right'caption='[[1ci9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=DFP:DIISOPROPYL PHOSPHONATE'>DFP</scene>
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<table><tr><td colspan='2'>[[1ci9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_gladioli Burkholderia gladioli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CI9 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE= ESTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28095 Burkholderia gladioli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DFP:DIISOPROPYL+PHOSPHONATE'>DFP</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ci9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ci9 OCA], [https://pdbe.org/1ci9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ci9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ci9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ci9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ESTB_BURGA ESTB_BURGA] Acts on short-chain (C4-C6) fatty acid esters and triglycerides, including tertiary alcohol esters. Activity on p-nitrophenyl esters is generally higher than on o-nitrophenyl esters. Lacks beta-lactamase activity; it hydrolyzes the ester bond of cephalosporin substrates but there is no opening of the beta-lactam ring observed.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/1ci9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ci9 ConSurf].
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<div style="clear:both"></div>
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'''DFP-INHIBITED ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI'''
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==See Also==
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*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Esterases form a diverse class of enzymes of largely unknown physiological role. Because many drugs and pesticides carry ester functions, the hydrolysis of such compounds forms at least one potential biological function. Carboxylesterases catalyze the hydrolysis of short chain aliphatic and aromatic carboxylic ester compounds. Esterases, D-alanyl-D-alanine-peptidases (DD-peptidases) and beta-lactamases can be grouped into two distinct classes of hydrolases with different folds and topologically unrelated catalytic residues, the one class comprising of esterases, the other one of beta-lactamases and DD-peptidases. The chemical reactivities of esters and beta-lactams towards hydrolysis are quite similar, which raises the question of which factors prevent esterases from displaying beta-lactamase activity and vice versa. Here we describe the crystal structure of EstB, an esterase isolated from Burkholderia gladioli. It shows the protein to belong to a novel class of esterases with homology to Penicillin binding proteins, notably DD-peptidase and class C beta-lactamases. Site-directed mutagenesis and the crystal structure of the complex with diisopropyl-fluorophosphate suggest Ser75 within the "beta-lactamase" Ser-x-x-Lys motif to act as catalytic nucleophile. Despite its structural homology to beta-lactamases, EstB shows no beta-lactamase activity. Although the nature and arrangement of active-site residues is very similar between EstB and homologous beta-lactamases, there are considerable differences in the shape of the active site tunnel. Modeling studies suggest steric factors to account for the enzyme's selectivity for ester hydrolysis versus beta-lactam cleavage.
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==About this Structure==
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1CI9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_gladioli Burkholderia gladioli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CI9 OCA].
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==Reference==
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EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity., Wagner UG, Petersen EI, Schwab H, Kratky C, Protein Sci. 2002 Mar;11(3):467-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11847270 11847270]
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[[Category: Burkholderia gladioli]]
[[Category: Burkholderia gladioli]]
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[[Category: Carboxylesterase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Kratky C]]
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[[Category: Kratky, C.]]
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[[Category: Petersen EI]]
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[[Category: Petersen, E I.]]
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[[Category: Schwab H]]
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[[Category: Schwab, H.]]
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[[Category: Wagner UG]]
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[[Category: Wagner, U G.]]
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[[Category: DFP]]
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[[Category: caboxylesterase]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:24:41 2008''
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Current revision

DFP-INHIBITED ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI

PDB ID 1ci9

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