4ivk: Difference between revisions
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==Crystal structure of a fammily VIII carboxylesterase in a complex with cephalothin.== | |||
<StructureSection load='4ivk' size='340' side='right' caption='[[4ivk]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ivk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IVK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CEP:CEPHALOTHIN+GROUP'>CEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ivi|4ivi]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ivk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ivk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ivk RCSB], [http://www.ebi.ac.uk/pdbsum/4ivk PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
EstU1 is a unique family VIII carboxylesterase that displays hydrolytic activity towards the amide bond of clinically used beta-lactam antibiotics as well as the ester bond of p-nitrophenyl esters. EstU1 assumes a beta-lactamase-like modular architecture and contains the residues Ser100, Lys103, and Tyr218, which correspond to the three catalytic residues (Ser64, Lys67, and Tyr150, respectively) of class C beta-lactamases. The structure of the EstU1/cephalothin complex demonstrates that the active site of EstU1 is not ideally tailored to perform an efficient deacylation reaction during the hydrolysis of beta-lactam antibiotics. This result explains the weak beta-lactamase activity of EstU1 compared with class C beta-lactamases. Finally, structural and sequential comparison of EstU1 with other family VIII carboxylesterases elucidates an operative molecular strategy used by family VIII carboxylesterases to extend their substrate spectrum. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. | |||
Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase.,Cha SS, Jun An Y, Jeong CS, Kim MK, Jeon JH, Lee CM, Lee HS, Gyun Kang S, Lee JH Proteins. 2013 Jun 5. doi: 10.1002/prot.24334. PMID:23737193<ref>PMID:23737193</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Carboxylesterase]] | [[Category: Carboxylesterase]] | ||
[[Category: Uncultured bacterium]] | [[Category: Uncultured bacterium]] | ||
[[Category: An, Y J | [[Category: An, Y J]] | ||
[[Category: Cha, S S | [[Category: Cha, S S]] | ||
[[Category: Jeong, C S | [[Category: Jeong, C S]] | ||
[[Category: Kim, M K | [[Category: Kim, M K]] | ||
[[Category: Deep sea sediment]] | [[Category: Deep sea sediment]] | ||
[[Category: Helical domain and a alpha/beta domain]] | [[Category: Helical domain and a alpha/beta domain]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||