==beta-fructosidase from Thermotoga maritima in complex with raffinose==

<StructureSection load='1w2t' size='340' side='right'caption='[[1w2t]], [[Resolution|resolution]] 1.87&Aring;' scene=''>

<table><tr><td colspan='2'>[[1w2t]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W2T FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</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=1w2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w2t OCA], [http://pdbe.org/1w2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w2t RCSB], [http://www.ebi.ac.uk/pdbsum/1w2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w2t ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Thermotoga maritima invertase (beta-fructosidase), a member of the glycoside hydrolase family GH-32, readily releases beta-D-fructose from sucrose, raffinose and fructan polymers such as inulin. These carbohydrates represent major carbon and energy sources for prokaryotes and eukaryotes. The invertase cleaves beta-fructopyranosidic linkages by a double-displacement mechanism, which involves a nucleophilic aspartate and a catalytic glutamic acid acting as a general acid/base. The three-dimensional structure of invertase shows a bimodular enzyme with a five bladed beta-propeller catalytic domain linked to a beta-sandwich of unknown function. In the present study we report the crystal structure of the inactivated invertase in interaction with the natural substrate molecule alpha-D-galactopyranosyl-(1,6)-alpha-D-glucopyranosyl-beta-D-fructofuranos ide (raffinose) at 1.87 A (1 A=0.1 nm) resolution. The structural analysis of the complex reveals the presence of three binding-subsites, which explains why T. maritima invertase exhibits a higher affinity for raffinose than sucrose, but a lower catalytic efficiency with raffinose as substrate than with sucrose.

Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose.,Alberto F, Jordi E, Henrissat B, Czjzek M Biochem J. 2006 May 1;395(3):457-62. PMID:16411890<ref>PMID:16411890</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1w2t" style="background-color:#fffaf0;"></div>

==See Also==

*[[Invertase|Invertase]]

== References ==

<references/>

[[Category: Beta-fructofuranosidase]]

[[Category: Thema]]

[[Category: Raffinose]]