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| | ==Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, in the apoprotein form== | | ==Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, in the apoprotein form== |
| - | <StructureSection load='4o8n' size='340' side='right' caption='[[4o8n]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='4o8n' size='340' side='right'caption='[[4o8n]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o8n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O8N FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O8N FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene><br> | + | </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=4o8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o8n OCA], [https://pdbe.org/4o8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o8n RCSB], [https://www.ebi.ac.uk/pdbsum/4o8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o8n ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o8o|4o8o]], [[4o8p|4o8p]]</td></tr>
| + | </table> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o8n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o8n RCSB], [http://www.ebi.ac.uk/pdbsum/4o8n PDBsum]</span></td></tr>
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| - | <table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Xylan debranching enzymes facilitate the complete hydrolysis of xylan and can be used to alter xylan chemistry. Herein, the GH62 family alpha-l-arabinofuranosidase from Streptomyces thermoviolaceus (SthAbf62A) was shown to have a half-life of 60 min at 60 degrees C, and ability to cleave alpha-1,3 l-arabinofuranose (l-Araf ) from singly-substituted xylopyranosyl (Xylp) backbone residues in wheat arabinoxylan; low activity towards arabinan as well as 4-nitrophenyl alpha-l-arabinofuranoside was also detected. After selectively removing alpha-1,3 l-Araf substituents from di-substituted Xylp residues present in wheat arabinoxylan, SthAbf62A could also cleave the remaining alpha-1,2 l-Araf substituents, confirming the ability of SthAbf62A to remove alpha-l-Araf residues that are (1-->2) and (1-->3) linked to mono-substituted beta-d-Xylp sugars. Three-dimensional structures of SthAbf62A and its complex with xylotetraose and l-arabinose confirmed a five-bladed beta-propeller fold and revealed a molecular Velcro in blade V between the beta1 and beta21 strands, a disulfide bond between Cys 27 and Cys 297, and a calcium ion coordinated in the central channel of the fold. The enzyme-arabinose complex structure further revealed a narrow and seemingly rigid l-arabinose binding pocket situated at the center of one side of the beta propeller, which stabilized the arabinofuranosyl substituent through several hydrogen-bonding and hydrophobic interactions. The predicted catalytic amino acids were oriented towards this binding pocket and the catalytic essentiality of Asp53 and Glu213 was confirmed by site-specific mutagenesis. Complex structures with xylotetraose revealed a shallow cleft for xylan backbone binding which is open at both ends and comprises multiple binding subsites above and flanking the l-arabinose binding pocket.
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| - | Biochemical and structural characterization of a thermostable family GH62 alpha-l-arabinofuranosidase from Streptomyces thermoviolaceus to elucidate the molecular basis for activity towards arabinoxylan.,Wang W, Mai-Gisondi G, Stogios PJ, Kaur A, Xu X, Cui H, Turunen O, Savchenko A, Master ER Appl Environ Microbiol. 2014 Jun 20. pii: AEM.00685-14. PMID:24951792<ref>PMID:24951792</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div> | + | |
| - | == References ==
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| - | <references/> | + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cui, H.]] | + | [[Category: Large Structures]] |
| - | [[Category: Master, E.]] | + | [[Category: Cui H]] |
| - | [[Category: Savchenko, A.]] | + | [[Category: Master E]] |
| - | [[Category: Stogios, P J.]] | + | [[Category: Savchenko A]] |
| - | [[Category: Wang, W.]] | + | [[Category: Stogios PJ]] |
| - | [[Category: Xu, X.]] | + | [[Category: Wang W]] |
| - | [[Category: 5-fold beta-propeller]]
| + | [[Category: Xu X]] |
| - | [[Category: Alpha-l-arabinofuranosidase]]
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| - | [[Category: Gh62]]
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| - | [[Category: Glycosyl hydrolase family 62]]
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| - | [[Category: Hydrolase]]
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