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| | <StructureSection load='5gmx' size='340' side='right'caption='[[5gmx]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5gmx' size='340' side='right'caption='[[5gmx]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gmx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultivated_bacterium Uncultivated bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GMX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GMX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gmx]] is a 2 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=5GMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GMX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PMS:PHENYLMETHANESULFONIC+ACID'>PMS</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=PMS:PHENYLMETHANESULFONIC+ACID'>PMS</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5gmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gmx OCA], [https://pdbe.org/5gmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gmx RCSB], [https://www.ebi.ac.uk/pdbsum/5gmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gmx ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gmx OCA], [http://pdbe.org/5gmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gmx RCSB], [http://www.ebi.ac.uk/pdbsum/5gmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gmx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0G2RKR9_9BACT A0A0G2RKR9_9BACT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carboxylesterase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Uncultivated bacterium]] | + | [[Category: Uncultured bacterium]] |
| - | [[Category: An, Y J]] | + | [[Category: An YJ]] |
| - | [[Category: Cha, S S]] | + | [[Category: Cha SS]] |
| - | [[Category: Estsrt1]]
| + | |
| - | [[Category: Extended spectrum beta-lactamase activity]]
| + | |
| - | [[Category: Flexibility]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A0A0G2RKR9_9BACT
Publication Abstract from PubMed
EstSRT1 is a family VIII carboxylesterase that hydrolyzes oxyimino third- and fourth-generation cephalosporins, first-generation cephalosporins and ester substrates. According to the crystal structure of EstSRT1 (2.0-A resolution), this protein contains a large alpha/beta domain and a small alpha-helical domain and harbors three catalytic residues (Ser71, Lys74, and Tyr160) in the cavity at the domain interface, similarly to other family VIII carboxylesterases. Comparison of the structures of EstSRT1 and EstU1, a family VIII carboxylesterase with no hydrolytic activity toward bulky oxyimino cephalosporins, revealed that EstSRT1 has a smaller active site, despite its extended substrate range. The B-factors of the active site segments that could potentially contact with the oxyimino groups and the R2 side chains of oxyimino cephalosporins are higher in EstSRT1 than in EstU1, thus suggesting the role of the active site's structural flexibility in the extension of EstSRT1's substrate spectrum.
Crystal structure of EstSRT1, a family VIII carboxylesterase displaying hydrolytic activity toward oxyimino cephalosporins.,Cha SS, An YJ Biochem Biophys Res Commun. 2016 Sep 16;478(2):818-24. doi:, 10.1016/j.bbrc.2016.08.031. Epub 2016 Aug 5. PMID:27501751[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cha SS, An YJ. Crystal structure of EstSRT1, a family VIII carboxylesterase displaying hydrolytic activity toward oxyimino cephalosporins. Biochem Biophys Res Commun. 2016 Sep 16;478(2):818-24. doi:, 10.1016/j.bbrc.2016.08.031. Epub 2016 Aug 5. PMID:27501751 doi:http://dx.doi.org/10.1016/j.bbrc.2016.08.031
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