3ug4: Difference between revisions

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'''Unreleased structure'''


The entry 3ug4 is ON HOLD
==Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex==
<StructureSection load='3ug4' size='340' side='right'caption='[[3ug4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ug4]] 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=3UG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UG4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=3ug4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ug4 OCA], [https://pdbe.org/3ug4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ug4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ug4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ug4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9WYB7_THEMA Q9WYB7_THEMA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors: Im, D.-H., Miyazaki, K., Wakagi, T., Fushinobu, S.
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>


Description: Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ug4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Fushinobu S]]
[[Category: Im D-H]]
[[Category: Miyazaki K]]
[[Category: Wakagi T]]

Latest revision as of 17:35, 1 November 2023

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

3ug4, resolution 2.15Å

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