4wlc: Difference between revisions
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''' | ==Structure of dextran glucosidase with glucose== | ||
<StructureSection load='4wlc' size='340' side='right' caption='[[4wlc]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4wlc]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WLC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='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=4wlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wlc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wlc RCSB], [http://www.ebi.ac.uk/pdbsum/4wlc 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: Complex]] | ||
[[Category: Dextran glucosidase]] | |||
[[Category: Glycoside hydrolase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Intermediate]] | |||
Revision as of 16:29, 26 August 2015
Structure of dextran glucosidase with glucoseStructure of dextran glucosidase with glucose
Structural highlights
Function[DEXB_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. References
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