4wlc: Difference between revisions

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'''Unreleased structure'''


The entry 4wlc is ON HOLD  until Paper Publication
==Structure of dextran glucosidase with glucose==
<StructureSection load='4wlc' size='340' side='right'caption='[[4wlc]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wlc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans_UA159 Streptococcus mutans UA159]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WLC 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]] 2.402&#8491;</td></tr>
<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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4wlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wlc OCA], [https://pdbe.org/4wlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wlc RCSB], [https://www.ebi.ac.uk/pdbsum/4wlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wlc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DEXB_STRMU DEXB_STRMU] The physiological substrates may be short isomaltosaccharides.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Streptococcus mutans dextran glucosidase (SmDG) belongs to glycoside hydrolase family 13, and catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form alpha-(1--&gt;6)-glucosidic linkage at the substrate non-reducing ends. Here, we report the 2.4A resolution crystal structure of glucosyl-enzyme intermediate of SmDG. In the obtained structure, the Trp238 side-chain that constitutes the substrate-binding site turned away from the active pocket, concurrently with conformational changes of the nucleophile and the acid/base residues. Different conformations of Trp238 in each reaction stage indicated its flexibility. Considering the results of kinetic analyses, such flexibility may reflect a requirement for the reaction mechanism of SmDG.


Authors: Kobayashi, M., Kato, K., Yao, M.
Structural insights into the catalytic reaction that is involved in the reorientation of Trp238 at the substrate-binding site in GH13 dextran glucosidase.,Kobayashi M, Saburi W, Nakatsuka D, Hondoh H, Kato K, Okuyama M, Mori H, Kimura A, Yao M FEBS Lett. 2015 Feb 13;589(4):484-9. doi: 10.1016/j.febslet.2015.01.005. Epub, 2015 Jan 14. PMID:25595454<ref>PMID:25595454</ref>


Description: structure of dextran glucosidase
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wlc" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus mutans UA159]]
[[Category: Kato K]]
[[Category: Kobayashi M]]
[[Category: Yao M]]
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