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| | ==Crystal structure of a family VIII carboxylesterase.== | | ==Crystal structure of a family VIII carboxylesterase.== |
| - | <StructureSection load='4ivi' size='340' side='right' caption='[[4ivi]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4ivi' size='340' side='right'caption='[[4ivi]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ivi]] 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=4IVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IVI FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ivk|4ivk]]</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> |
| - | <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=4ivi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ivi OCA], [http://pdbe.org/4ivi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ivi RCSB], [http://www.ebi.ac.uk/pdbsum/4ivi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ivi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | ==See Also== | | ==See Also== |
| - | *[[Carboxylesterase|Carboxylesterase]] | + | *[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carboxylesterase]] | + | [[Category: Large Structures]] |
| | [[Category: Uncultured bacterium]] | | [[Category: Uncultured bacterium]] |
| - | [[Category: An, Y J]] | + | [[Category: An YJ]] |
| - | [[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: Carboxylesterases beta-lactamase]]
| + | |
| - | [[Category: Deep sea sediment]]
| + | |
| - | [[Category: Helical domain and a alpha/beta domain]]
| + | |
| - | [[Category: Hydrolase]]
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| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cha SS, Jun An Y, Jeong CS, Kim MK, Jeon JH, Lee CM, Lee HS, Gyun Kang S, Lee JH. Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase. Proteins. 2013 Jun 5. doi: 10.1002/prot.24334. PMID:23737193 doi:http://dx.doi.org/10.1002/prot.24334
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