5mif

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==Crystal structure of carboxyl esterase 2 (TmelEST2) from mycorrhizal fungus Tuber melanosporum==
==Crystal structure of carboxyl esterase 2 (TmelEST2) from mycorrhizal fungus Tuber melanosporum==
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<StructureSection load='5mif' size='340' side='right' caption='[[5mif]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
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<StructureSection load='5mif' size='340' side='right'caption='[[5mif]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5mif]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MIF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MIF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5mif]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Tuber_melanosporum_Mel28 Tuber melanosporum Mel28]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MIF 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=TRT:FRAGMENT+OF+TRITON+X-100'>TRT</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]] 2.141&#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=5mif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mif OCA], [http://pdbe.org/5mif PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mif RCSB], [http://www.ebi.ac.uk/pdbsum/5mif PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mif 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=TRT:FRAGMENT+OF+TRITON+X-100'>TRT</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=5mif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mif OCA], [https://pdbe.org/5mif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mif RCSB], [https://www.ebi.ac.uk/pdbsum/5mif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mif 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/D5GA36_TUBMM D5GA36_TUBMM]
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An increasing number of esterases is being revealed by (meta) genomic sequencing projects, but few of them are functionally/structurally characterized, especially enzymes of fungal origin. Starting from a three-member gene family of secreted putative "lipases/esterases" preferentially expressed in the symbiotic phase of the mycorrhizal fungus Tuber melanosporum ("black truffle"), we show here that these enzymes (TmelEST1-3) are dimeric, heat-resistant carboxylesterases capable of hydrolyzing various short/medium chain p-nitrophenyl esters. TmelEST2 was the most active (kcat = 2302 s-1 for p-nitrophenyl-butyrate) and thermally stable (T50 = 68.3 degrees C), while TmelEST3 was the only one displaying some activity on tertiary alcohol esters. X-ray diffraction analysis of TmelEST2 revealed a classical alpha/beta hydrolase-fold structure, with a network of dimer-stabilizing intermolecular interactions typical of archaea esterases. The predicted structures of TmelEST1 and 3 are overall quite similar to that of TmelEST2 but with some important differences. Most notably, the much smaller volume of the substrate-binding pocket and the more acidic electrostatic surface profile of TmelEST1. This was also the only TmelEST capable of hydrolyzing feruloyl-esters, suggestinng a possible role in root cell-wall deconstruction during symbiosis establishment. In addition to their potential biotechnological interest, TmelESTs raise important questions regarding the evolutionary recruitment of archaea-like enzymes into mesophilic subterranean fungi such as truffles.
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A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mychorrizal fungus Tuber melanosporum.,Cavazzini D, Grossi G, Levati E, Vallese F, Montanini B, Bolchi A, Zanotti G, Ottonello S Sci Rep. 2017 Aug 9;7(1):7628. doi: 10.1038/s41598-017-08007-9. PMID:28794466<ref>PMID:28794466</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 5mif" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cavazzini, D]]
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[[Category: Large Structures]]
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[[Category: Ottonello, S]]
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[[Category: Tuber melanosporum Mel28]]
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[[Category: Valesse, F]]
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[[Category: Cavazzini D]]
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[[Category: Zanotti, G]]
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[[Category: Ottonello S]]
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[[Category: Hydrolase]]
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[[Category: Vallese F]]
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[[Category: Lipase alpha/beta hydrolase fold archaebacterial-like enzyme]]
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[[Category: Zanotti G]]

Current revision

Crystal structure of carboxyl esterase 2 (TmelEST2) from mycorrhizal fungus Tuber melanosporum

PDB ID 5mif

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