4xb3: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='4xb3' size='340' side='right'caption='[[4xb3]], [[Resolution|resolution]] 2.09Å' scene=''> | <StructureSection load='4xb3' size='340' side='right'caption='[[4xb3]], [[Resolution|resolution]] 2.09Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xb3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xb3]] 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=4XB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XB3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</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=4xb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xb3 OCA], [https://pdbe.org/4xb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xb3 RCSB], [https://www.ebi.ac.uk/pdbsum/4xb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xb3 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/DEXB_STRMU DEXB_STRMU] The physiological substrates may be short isomaltosaccharides. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 27: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptococcus mutans UA159]] | ||
[[Category: Kato | [[Category: Kato K]] | ||
[[Category: Kobayashi | [[Category: Kobayashi M]] | ||
[[Category: Yao | [[Category: Yao M]] | ||
Revision as of 00:20, 13 April 2023
Structure of dextran glucosidaseStructure of dextran glucosidase
Structural highlights
FunctionDEXB_STRMU The physiological substrates may be short isomaltosaccharides. Publication Abstract from PubMedStreptococcus 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-->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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||