1llb: Difference between revisions
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New page: left|200px<br /><applet load="1llb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1llb, resolution 1.72Å" /> '''Crystal Structure Of... |
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== | ==Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With ATMO-penicillin== | ||
beta-lactamases confer resistance to beta-lactam antibiotics such as | <StructureSection load='1llb' size='340' side='right'caption='[[1llb]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72Å</td></tr> | |||
<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> | |||
<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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1llb_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[ | <div class="pdbe-citations 1llb" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Blaszczak | [[Category: Blaszczak LC]] | ||
[[Category: Morandi | [[Category: Morandi F]] | ||
[[Category: Shoichet | [[Category: Shoichet BK]] | ||
[[Category: Trehan | [[Category: Trehan I]] | ||
Latest revision as of 08:37, 6 November 2024
Crystal Structure Of AmpC beta-Lactamase From E. Coli In Complex With ATMO-penicillin
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