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4q05

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<StructureSection load='4q05' size='340' side='right'caption='[[4q05]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='4q05' size='340' side='right'caption='[[4q05]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4q05]] 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=4Q05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q05 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4q05]] 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=4Q05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q05 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
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<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=4q05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q05 OCA], [http://pdbe.org/4q05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q05 RCSB], [http://www.ebi.ac.uk/pdbsum/4q05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q05 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4q05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q05 OCA], [https://pdbe.org/4q05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q05 RCSB], [https://www.ebi.ac.uk/pdbsum/4q05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q05 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/B8Y553_9BACT B8Y553_9BACT]
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Hormone-sensitive lipases (HSLs) are widely distributed in microorganisms, plants, and animals. Microbial HSLs are classified into two subfamilies, an unnamed new subfamily and the GDSAG motif subfamily. Due to the lack of structural information, the detailed catalytic mechanism of the new subfamily is not yet clarified. Based on sequence analysis, we propose to name the new subfamily as the GTSAG motif subfamily. We identified a novel HSL esterase E25, a member of the GTSAG motif subfamily, by functional metagenomic screening, and resolved its structure at 2.05 A. E25 is mesophilic (optimum temperature at 50 degrees C), salt-tolerant, slightly alkaline (optimum pH at 8.5) for its activity, and capable of hydrolyzing short chain monoesters (C2-C10). E25 tends to form dimers both in the crystal and in solution. An E25 monomer contains an N-terminal CAP domain, and a classical alpha/beta hydrolase-fold domain. Residues Ser(186), Asp(282), and His(312) comprise the catalytic triad. Structural and mutational analyses indicated that E25 adopts a dimerization pattern distinct from other HSLs. E25 dimer is mainly stabilized by an N-terminal loop intersection from the CAP domains and hydrogen bonds and salt bridges involving seven highly conserved hydrophilic residues from the catalytic domains. Further analysis indicated that E25 also has some catalytic profiles different from other HSLs. Dimerization is essential for E25 to exert its catalytic activity by keeping the accurate orientation of the catalytic Asp(282) within the catalytic triad. Our results reveal the structural basis for dimerization and catalysis of an esterase from the GTSAG motif subfamily of the HSL family.
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Structural basis for dimerization and catalysis of a novel esterase from the GTSAG motif subfamily of the bacterial hormone-sensitive lipase family.,Li PY, Ji P, Li CY, Zhang Y, Wang GL, Zhang XY, Xie BB, Qin QL, Chen XL, Zhou BC, Zhang YZ J Biol Chem. 2014 Jul 4;289(27):19031-41. doi: 10.1074/jbc.M114.574913. Epub 2014, May 27. PMID:24867954<ref>PMID:24867954</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4q05" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Uncultivated bacterium]]
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[[Category: Uncultured bacterium]]
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[[Category: Li, C Y]]
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[[Category: Li CY]]
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[[Category: Li, P Y]]
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[[Category: Li PY]]
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[[Category: Zhang, Y Z]]
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[[Category: Zhang YZ]]
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[[Category: Esterase]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of an esterase E25

PDB ID 4q05

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