1llb

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[[Image:1llb.gif|left|200px]]
 
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{{Structure
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==Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With ATMO-penicillin==
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|PDB= 1llb |SIZE=350|CAPTION= <scene name='initialview01'>1llb</scene>, resolution 1.72&Aring;
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<StructureSection load='1llb' size='340' side='right'caption='[[1llb]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PCN:2-{1-[2-(2-AMINO-THIAZOL-4-YL)-2-METHOXYIMINO-ACETYLAMINO]-2-OXO-ETHYL}-5,5-DIMETHYL-THIAZOLIDINE-4-CARBOXYLIC+ACID'>PCN</scene>
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<table><tr><td colspan='2'>[[1llb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLB 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]] 1.72&#8491;</td></tr>
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|GENE= ampC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCN:2-{1-[2-(2-AMINO-THIAZOL-4-YL)-2-METHOXYIMINO-ACETYLAMINO]-2-OXO-ETHYL}-5,5-DIMETHYL-THIAZOLIDINE-4-CARBOXYLIC+ACID'>PCN</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=1llb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llb OCA], [https://pdbe.org/1llb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1llb RCSB], [https://www.ebi.ac.uk/pdbsum/1llb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llb ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ke4|1KE4]], [[1iel|1IEL]], [[1iem|1IEM]], [[1fcn|1FCN]], [[1kvm|1KVM]], [[1fr6|1FR6]], [[1ll9|1LL9]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1llb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llb OCA], [http://www.ebi.ac.uk/pdbsum/1llb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1llb RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
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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/ll/1llb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1llb ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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beta-lactamases confer resistance to beta-lactam antibiotics such as penicillins and cephalosporins. However, beta-lactams that form an acyl-intermediate with the enzyme but subsequently are hindered from forming a catalytically competent conformation seem to be inhibitors of beta-lactamases. This inhibition may be imparted by specific groups on the ubiquitous R(1) side chain of beta-lactams, such as the 2-amino-4-thiazolyl methoxyimino (ATMO) group common among third-generation cephalosporins. Using steric hindrance of deacylation as a design guide, penicillin and carbacephem substrates were converted into effective beta-lactamase inhibitors and antiresistance antibiotics. To investigate the structural bases of inhibition, the crystal structures of the acyl-adducts of the penicillin substrate amoxicillin and the new analogous inhibitor ATMO-penicillin were determined. ATMO-penicillin binds in a catalytically incompetent conformation resembling that adopted by third-generation cephalosporins, demonstrating the transferability of such sterically hindered groups in inhibitor design.
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'''Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With ATMO-penicillin'''
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Using steric hindrance to design new inhibitors of class C beta-lactamases.,Trehan I, Morandi F, Blaszczak LC, Shoichet BK Chem Biol. 2002 Sep;9(9):971-80. PMID:12323371<ref>PMID:12323371</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1llb" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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beta-lactamases confer resistance to beta-lactam antibiotics such as penicillins and cephalosporins. However, beta-lactams that form an acyl-intermediate with the enzyme but subsequently are hindered from forming a catalytically competent conformation seem to be inhibitors of beta-lactamases. This inhibition may be imparted by specific groups on the ubiquitous R(1) side chain of beta-lactams, such as the 2-amino-4-thiazolyl methoxyimino (ATMO) group common among third-generation cephalosporins. Using steric hindrance of deacylation as a design guide, penicillin and carbacephem substrates were converted into effective beta-lactamase inhibitors and antiresistance antibiotics. To investigate the structural bases of inhibition, the crystal structures of the acyl-adducts of the penicillin substrate amoxicillin and the new analogous inhibitor ATMO-penicillin were determined. ATMO-penicillin binds in a catalytically incompetent conformation resembling that adopted by third-generation cephalosporins, demonstrating the transferability of such sterically hindered groups in inhibitor design.
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1LLB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLB OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Using steric hindrance to design new inhibitors of class C beta-lactamases., Trehan I, Morandi F, Blaszczak LC, Shoichet BK, Chem Biol. 2002 Sep;9(9):971-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12323371 12323371]
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[[Category: Beta-lactamase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Blaszczak, L C.]]
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[[Category: Blaszczak LC]]
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[[Category: Morandi, F.]]
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[[Category: Morandi F]]
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[[Category: Shoichet, B K.]]
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[[Category: Shoichet BK]]
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[[Category: Trehan, I.]]
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[[Category: Trehan I]]
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[[Category: beta-lactamase]]
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[[Category: cephalosporinase]]
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[[Category: hydrolase]]
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[[Category: serine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:13 2008''
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Current revision

Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With ATMO-penicillin

PDB ID 1llb

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