4ivi: Difference between revisions
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The | ==Crystal structure of a family VIII carboxylesterase.== | ||
<StructureSection load='4ivi' size='340' side='right'caption='[[4ivi]], [[Resolution|resolution]] 2.00Å' 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]] 2Å</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> | |||
<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> | |||
<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]] | |||
Latest revision as of 03:03, 21 November 2024
Crystal structure of a family VIII carboxylesterase.
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