1i2s

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[[Image:1i2s.jpg|left|200px]]
 
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{{Structure
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==BETA-LACTAMASE FROM BACILLUS LICHENIFORMIS BS3==
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|PDB= 1i2s |SIZE=350|CAPTION= <scene name='initialview01'>1i2s</scene>, resolution 1.70&Aring;
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<StructureSection load='1i2s' size='340' side='right'caption='[[1i2s]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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<table><tr><td colspan='2'>[[1i2s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I2S FirstGlance]. <br>
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|ACTIVITY= <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>
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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]] 1.7&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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|DOMAIN=
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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=1i2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i2s OCA], [https://pdbe.org/1i2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i2s RCSB], [https://www.ebi.ac.uk/pdbsum/1i2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i2s ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1i2w|1I2W]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i2s OCA], [http://www.ebi.ac.uk/pdbsum/1i2s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i2s RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/BLAC_BACLI BLAC_BACLI]
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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/i2/1i2s_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=1i2s ConSurf].
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<div style="clear:both"></div>
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'''BETA-LACTAMASE FROM BACILLUS LICHENIFORMIS BS3'''
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The Bacillus licheniformis BS3 beta-lactamase catalyzes the hydrolysis of the beta-lactam ring of penicillins, cephalosporins, and related compounds. The production of beta-lactamases is the most common and thoroughly studied cause of antibiotic resistance. Although they escape the hydrolytic activity of the prototypical Staphylococcus aureus beta-lactamase, many cephems are good substrates for a large number of beta-lactamases. However, the introduction of a 7alpha-methoxy substituent, as in cefoxitin, extends their antibacterial spectrum to many cephalosporin-resistant Gram-negative bacteria. The 7alpha-methoxy group selectively reduces the hydrolytic action of many beta-lactamases without having a significant effect on the affinity for the target enzymes, the membrane penicillin-binding proteins. We report here the crystallographic structures of the BS3 enzyme and its acyl-enzyme adduct with cefoxitin at 1.7 A resolution. The comparison of the two structures reveals a covalent acyl-enzyme adduct with perturbed active site geometry, involving a different conformation of the omega-loop that bears the essential catalytic Glu166 residue. This deformation is induced by the cefoxitin side chain whose position is constrained by the presence of the alpha-methoxy group. The hydrolytic water molecule is also removed from the active site by the 7beta-carbonyl of the acyl intermediate. In light of the interactions and steric hindrances in the active site of the structure of the BS3-cefoxitin acyl-enzyme adduct, the crucial role of the conserved Asn132 residue is confirmed and a better understanding of the kinetic results emerges.
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==About this Structure==
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1I2S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I2S OCA].
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==Reference==
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Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin., Fonze E, Vanhove M, Dive G, Sauvage E, Frere JM, Charlier P, Biochemistry. 2002 Feb 12;41(6):1877-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11827533 11827533]
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[[Category: Bacillus licheniformis]]
[[Category: Bacillus licheniformis]]
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[[Category: Beta-lactamase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Charlier P]]
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[[Category: Charlier, P.]]
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[[Category: Dive G]]
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[[Category: Dive, G.]]
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[[Category: Fonze E]]
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[[Category: Fonze, E.]]
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[[Category: Frere JM]]
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[[Category: Frere, J M.]]
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[[Category: Sauvage E]]
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[[Category: Sauvage, E.]]
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[[Category: Vanhove M]]
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[[Category: Vanhove, M.]]
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[[Category: antibiotic resistance]]
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[[Category: hydrolase]]
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[[Category: serine beta-lactamase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:13:49 2008''
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Current revision

BETA-LACTAMASE FROM BACILLUS LICHENIFORMIS BS3

PDB ID 1i2s

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