7zon
From Proteopedia
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| - | ==Carbohydrate binding domain | + | ==Carbohydrate binding domain CBM92-B from a multi-catalytic glucanase-chitinase from Chitinophaga pinensis DSM 2588 in complex with glucose== |
<StructureSection load='7zon' size='340' side='right'caption='[[7zon]], [[Resolution|resolution]] 1.77Å' scene=''> | <StructureSection load='7zon' size='340' side='right'caption='[[7zon]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7zon]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chitinophaga_pinensis_DSM_2588 Chitinophaga pinensis DSM 2588]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZON FirstGlance]. <br> | <table><tr><td colspan='2'>[[7zon]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chitinophaga_pinensis_DSM_2588 Chitinophaga pinensis DSM 2588]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZON FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</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]] 1.77Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</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=7zon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zon OCA], [https://pdbe.org/7zon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zon RCSB], [https://www.ebi.ac.uk/pdbsum/7zon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zon ProSAT]</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=7zon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zon OCA], [https://pdbe.org/7zon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zon RCSB], [https://www.ebi.ac.uk/pdbsum/7zon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zon ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A979GQH9_CHIPD A0A979GQH9_CHIPD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Carbohydrate-binding modules (CBMs) are non-catalytic proteins found appended to carbohydrate-active enzymes. Soil and marine bacteria secrete such enzymes to scavenge nutrition, and they often use CBMs to improve reaction rates and retention of released sugars. Here we present a structural and functional analysis of the recently established CBM family 92. All proteins analysed bind preferentially to beta-1,6-glucans. This contrasts with the diversity of predicted substrates among the enzymes attached to CBM92 domains. We present crystal structures for two proteins, and confirm by mutagenesis that tryptophan residues permit ligand binding at three distinct functional binding sites on each protein. Multivalent CBM families are uncommon, so the establishment and structural characterisation of CBM92 enriches the classification database and will facilitate functional prediction in future projects. We propose that CBM92 proteins may cross-link polysaccharides in nature, and might have use in novel strategies for enzyme immobilisation. | ||
| + | |||
| + | Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to beta-glucans.,Hao MS, Mazurkewich S, Li H, Kvammen A, Saha S, Koskela S, Inman AR, Nakajima M, Tanaka N, Nakai H, Branden G, Bulone V, Larsbrink J, McKee LS Nat Commun. 2024 Apr 23;15(1):3429. doi: 10.1038/s41467-024-47584-y. PMID:38653764<ref>PMID:38653764</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7zon" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Carbohydrate binding domain CBM92-B from a multi-catalytic glucanase-chitinase from Chitinophaga pinensis DSM 2588 in complex with glucose
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