View source for 4ivi


==Crystal structure of a family VIII carboxylesterase.==
<StructureSection load='4ivi' size='340' side='right'caption='[[4ivi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ivi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IVI 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4ivi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ivi OCA], [https://pdbe.org/4ivi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ivi RCSB], [https://www.ebi.ac.uk/pdbsum/4ivi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ivi ProSAT]</span></td></tr>
</table>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4ivi" style="background-color:#fffaf0;"></div>

==See Also==
*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Uncultured bacterium]]
[[Category: An YJ]]
[[Category: Cha S-S]]
[[Category: Jeong C-S]]
[[Category: Kim M-K]]