5h4r: Difference between revisions
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<StructureSection load='5h4r' size='340' side='right'caption='[[5h4r]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5h4r' size='340' side='right'caption='[[5h4r]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5h4r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H4R OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5h4r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldicellulosiruptor_sp._F32 Caldicellulosiruptor sp. F32]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H4R FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7031044Å</td></tr> | ||
<tr id=' | <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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900011:beta-cellotetraose'>PRD_900011</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5h4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h4r OCA], [https://pdbe.org/5h4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h4r RCSB], [https://www.ebi.ac.uk/pdbsum/5h4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h4r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/R9RX81_9FIRM R9RX81_9FIRM] | |||
<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: Caldicellulosiruptor sp. F32]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dong | [[Category: Dong S]] | ||
[[Category: Feng | [[Category: Feng Y]] | ||
[[Category: Liu | [[Category: Liu X]] | ||
[[Category: Wang | [[Category: Wang X]] | ||
[[Category: Zhou | [[Category: Zhou H]] | ||
Latest revision as of 10:23, 9 August 2023
the complex of Glycoside Hydrolase 5 Lichenase from Caldicellulosiruptor sp. F32 E188Q mutant and cellotetraosethe complex of Glycoside Hydrolase 5 Lichenase from Caldicellulosiruptor sp. F32 E188Q mutant and cellotetraose
Structural highlights
FunctionPublication Abstract from PubMedGlycoside hydrolase (GH) family 5 is one of the largest GH families with various GH activities including lichenase, but the structural basis of the GH5 lichenase activity is still unknown. A novel thermostable lichenase F32EG5 belonging to GH5 was identified from an extremely thermophilic bacterium Caldicellulosiruptor sp. F32. F32EG5 is a bi-functional cellulose and lichenan-degrading enzyme and exhibited a high activity on beta-1,3-1,4-glucan but side activity on cellulose. Thin-layer chromatography and NMR analyses indicated that F32EG5 cleaved the beta-1,4 linkage or the beta-1,3 linkage while a 4- O -substitued glucose residue linked to a glucose residue through a beta-1,3 linkage, which is completely different from extensively studied GH16 lichenase that catalyses strict endo-hydrolysis of the beta-1,4-glycosidic linkage adjacent to a 3- O -substitued glucose residue in the mixed linked beta-glucans. The crystal structure of F32EG5 was determined to 2.8 A resolution and the crystal structure of the complex of F32EG5 E193Q mutant and cellotetraose was determined to 1.7 A resolution, which revealed that the exit subsites of substrate binding sites contribute to both thermostability and substrate specificity of F32EG5. The sugar chain showed a sharp bend in the complex structure, suggesting that a substrate cleft fitting to the bent sugar chains in lichenan is a common feature of GH5 lichenases. The mechanism of thermostability and substrate selectivity of F32EG5 was further demonstrated by molecular dynamics simulation and site-directed mutagenesis. These results provide biochemical and structural insight into thermostability and substrate selectivity of GH5 lichenases which have potential in industrial processes. Structural Insights into the Substrate Specificity of a Glycoside Hydrolase Family 5 Lichenase from Caldicellulosiruptor sp. F32.,Meng DD, Liu X, Dong S, Wang YF, Ma XQ, Zhou H, Wang X, Yao LS, Feng Y, Li FL Biochem J. 2017 Aug 24. pii: BCJ20170328. doi: 10.1042/BCJ20170328. PMID:28838949[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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