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3ug5

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'''Unreleased structure'''
 
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The entry 3ug5 is ON HOLD until Paper Publication
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==Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex==
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<StructureSection load='3ug5' size='340' side='right'caption='[[3ug5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ug5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UG5 FirstGlance]. <br>
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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]] 2.3&#8491;</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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</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=3ug5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ug5 OCA], [https://pdbe.org/3ug5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ug5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ug5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ug5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9WYB7_THEMA Q9WYB7_THEMA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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alpha-L-Arabinofuranosidase from the hyperthermophilic bacterium Thermotoga maritima (Tm-AFase) is an extremely thermophilic enzyme belonging to glycoside hydrolase family 51. It can catalyze the transglycosylation of a novel glycosyl donor, 4,6-dimethoxy-1,3,5-triazin-2-yl (DMT)-beta-D-xylopyranoside. In this study we determined the crystal structures of Tm-AFase in substrate-free and complex forms with arabinose and xylose at 1.8-2.3 A resolution to determine the architecture of the substrate binding pocket. Subsite -1 of Tm-AFase is similar to that of alpha-L-arabinofuranosidase from Geobacillus stearothermophilus, but the substrate binding pocket of Tm-AFase is narrower and more hydrophobic. Possible substrate binding modes were investigated by automated docking analysis.
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Authors: Im, D.-H., Miyazaki, K., Wakagi, T., Fushinobu, S.
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Crystal Structures of Glycoside Hydrolase Family 51 alpha-L-Arabinofuranosidase from Thermotoga maritima.,Im DH, Kimura K, Hayasaka F, Tanaka T, Noguchi M, Kobayashi A, Shoda S, Miyazaki K, Wakagi T, Fushinobu S Biosci Biotechnol Biochem. 2012 Feb 23;76(2):423-8. Epub 2012 Feb 7. PMID:22313787<ref>PMID:22313787</ref>
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Description: Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex
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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 3ug5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermotoga maritima]]
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[[Category: Fushinobu S]]
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[[Category: Im D-H]]
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[[Category: Miyazaki K]]
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[[Category: Wakagi T]]

Current revision

Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex

PDB ID 3ug5

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