4ivk
From Proteopedia
(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]] | ||
Revision as of 12:24, 21 December 2014
Crystal structure of a fammily VIII carboxylesterase in a complex with cephalothin.
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