4xb3
From Proteopedia
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| - | ''' | + | ==Structure of dextran glucosidase== |
| + | <StructureSection load='4xb3' size='340' side='right' caption='[[4xb3]], [[Resolution|resolution]] 2.09Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xb3]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucan_1,6-alpha-glucosidase Glucan 1,6-alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.70 3.2.1.70] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xb3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xb3 RCSB], [http://www.ebi.ac.uk/pdbsum/4xb3 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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-->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<ref>PMID:25595454</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Glucan 1,6-alpha-glucosidase]] | ||
| + | [[Category: Kato, K]] | ||
[[Category: Kobayashi, M]] | [[Category: Kobayashi, M]] | ||
[[Category: Yao, M]] | [[Category: Yao, M]] | ||
| - | [[Category: | + | [[Category: Dextran glucosidase]] |
| + | [[Category: Glycoside hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Intermediate]] | ||
Revision as of 13:24, 26 August 2015
Structure of dextran glucosidase
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