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==GH6 Orpinomyces sp. Y102 enzyme==
==GH6 Orpinomyces sp. Y102 enzyme==
<StructureSection load='6idw' size='340' side='right' caption='[[6idw]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
<StructureSection load='6idw' size='340' side='right'caption='[[6idw]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6idw]] is a 4 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5jx6 5jx6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IDW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IDW FirstGlance]. <br>
<table><tr><td colspan='2'>[[6idw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Orpinomyces_sp._Y102 Orpinomyces sp. Y102]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5jx6 5jx6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IDW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.78&#8491;</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=6idw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6idw OCA], [http://pdbe.org/6idw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6idw RCSB], [http://www.ebi.ac.uk/pdbsum/6idw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6idw ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</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=6idw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6idw OCA], [https://pdbe.org/6idw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6idw RCSB], [https://www.ebi.ac.uk/pdbsum/6idw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6idw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A076U926_9FUNG A0A076U926_9FUNG]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The catalytic domain (residues 128-449) of the Orpinomyces sp. Y102 CelC7 enzyme (Orp CelC7) exhibits cellobiohydrolase and cellotriohydrolase activities. Crystal structures of Orp CelC7 and its cellobiose-bound complex have been solved at resolutions of 1.80 and 2.78 A, respectively. Cellobiose occupies subsites +1 and +2 within the active site of Orp CelC7 and forms hydrogen bonds to two key residues: Asp248 and Asp409. Furthermore, its substrate-binding sites have both tunnel-like and open-cleft conformations, suggesting that the glycoside hydrolase family 6 (GH6) Orp CelC7 enzyme may perform enzymatic hydrolysis in the same way as endoglucanases and cellobiohydrolases. LC-MS/MS analysis revealed cellobiose (major) and cellotriose (minor) to be the respective products of endo and exo activity of the GH6 Orp CelC7.
Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose.,Huang HC, Qi LH, Chen YC, Tsai LC Acta Crystallogr D Struct Biol. 2019 Dec 1;75(Pt 12):1138-1147. doi:, 10.1107/S2059798319013597. Epub 2019 Nov 29. PMID:31793907<ref>PMID:31793907</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6idw" style="background-color:#fffaf0;"></div>
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Huang, H C]]
[[Category: Large Structures]]
[[Category: Tsai, L C]]
[[Category: Orpinomyces sp. Y102]]
[[Category: Cbh7]]
[[Category: Huang HC]]
[[Category: Endoglucanase]]
[[Category: Tsai LC]]
[[Category: Exoglucanase]]
[[Category: Gh6]]
[[Category: Hydrolase]]
[[Category: Orpinomyces sp]]

Latest revision as of 12:38, 22 November 2023

GH6 Orpinomyces sp. Y102 enzymeGH6 Orpinomyces sp. Y102 enzyme

Structural highlights

6idw is a 4 chain structure with sequence from Orpinomyces sp. Y102. This structure supersedes the now removed PDB entry 5jx6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.78Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A076U926_9FUNG

Publication Abstract from PubMed

The catalytic domain (residues 128-449) of the Orpinomyces sp. Y102 CelC7 enzyme (Orp CelC7) exhibits cellobiohydrolase and cellotriohydrolase activities. Crystal structures of Orp CelC7 and its cellobiose-bound complex have been solved at resolutions of 1.80 and 2.78 A, respectively. Cellobiose occupies subsites +1 and +2 within the active site of Orp CelC7 and forms hydrogen bonds to two key residues: Asp248 and Asp409. Furthermore, its substrate-binding sites have both tunnel-like and open-cleft conformations, suggesting that the glycoside hydrolase family 6 (GH6) Orp CelC7 enzyme may perform enzymatic hydrolysis in the same way as endoglucanases and cellobiohydrolases. LC-MS/MS analysis revealed cellobiose (major) and cellotriose (minor) to be the respective products of endo and exo activity of the GH6 Orp CelC7.

Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose.,Huang HC, Qi LH, Chen YC, Tsai LC Acta Crystallogr D Struct Biol. 2019 Dec 1;75(Pt 12):1138-1147. doi:, 10.1107/S2059798319013597. Epub 2019 Nov 29. PMID:31793907[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Huang HC, Qi LH, Chen YC, Tsai LC. Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose. Acta Crystallogr D Struct Biol. 2019 Dec 1;75(Pt 12):1138-1147. doi:, 10.1107/S2059798319013597. Epub 2019 Nov 29. PMID:31793907 doi:http://dx.doi.org/10.1107/S2059798319013597

6idw, resolution 2.78Å

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