3vup: Difference between revisions
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[[ | ==Beta-1,4-mannanase from the common sea hare Aplysia kurodai== | ||
<StructureSection load='3vup' size='340' side='right' caption='[[3vup]], [[Resolution|resolution]] 1.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vup]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aplysia_kurodai Aplysia kurodai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VUP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VUP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vup OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vup RCSB], [http://www.ebi.ac.uk/pdbsum/3vup PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
beta-1,4-Mannanase (EC 3.2.1.78) catalyzes the hydrolysis of beta-1,4-glycosidic bonds within mannan, a major constituent group of the hemicelluloses. Bivalves and gastropods possess beta-1,4-mannanase and may degrade mannan in seaweed and/or phytoplankton to obtain carbon and energy using the secreted enzymes in their digestive systems. In the present study, the crystal structure of AkMan, a gastropod beta-1,4-mannanase prepared from the common sea hare Aplysia kurodai, was determined at 1.05 A resolution. This is the first report of the three-dimensional structure of a gastropod beta-1,4-mannanase. The structure was compared with bivalve beta-1,4-mannanase and the roles of residues in the catalytic cleft were investigated. No obvious binding residue was found in subsite +1 and the substrate-binding site was exposed to the molecular surface, which may account for the enzymatic properties of mannanases that can digest complex substrates such as glucomannan and branched mannan. | |||
Structure of beta-1,4-mannanase from the common sea hare Aplysia kurodai at 1.05 A resolution.,Mizutani K, Tsuchiya S, Toyoda M, Nanbu Y, Tominaga K, Yuasa K, Takahashi N, Tsuji A, Mikami B Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1164-8., doi: 10.1107/S1744309112037074. Epub 2012 Sep 25. PMID:23027740<ref>PMID:23027740</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Aplysia kurodai]] | [[Category: Aplysia kurodai]] | ||
[[Category: Mikami, B | [[Category: Mikami, B]] | ||
[[Category: Mizutani, K | [[Category: Mizutani, K]] | ||
[[Category: Nanbu, Y | [[Category: Nanbu, Y]] | ||
[[Category: Takahashi, N | [[Category: Takahashi, N]] | ||
[[Category: Tominaga, K | [[Category: Tominaga, K]] | ||
[[Category: Toyoda, M | [[Category: Toyoda, M]] | ||
[[Category: Tsuchiya, S | [[Category: Tsuchiya, S]] | ||
[[Category: Tsuji, A | [[Category: Tsuji, A]] | ||
[[Category: Yuasa, K | [[Category: Yuasa, K]] | ||
[[Category: 4-mannanase]] | [[Category: 4-mannanase]] | ||
[[Category: Beta-1]] | [[Category: Beta-1]] | ||
Revision as of 07:57, 20 January 2015
Beta-1,4-mannanase from the common sea hare Aplysia kurodai
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