2inu
From Proteopedia
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| - | [[Image:2inu.jpg|left|200px]]<br /><applet load="2inu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2inu, resolution 1.8Å" /> | ||
| - | '''Crystal structure of inulin fructotransferase in the absence of substrate'''<br /> | ||
| - | == | + | ==Crystal structure of Inulin fructotransferase in the absence of substrate== |
| - | + | <StructureSection load='2inu' size='340' side='right'caption='[[2inu]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | [[ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[2inu]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_sp._snu-7 Bacillus sp. snu-7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2INU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2INU FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PO:PHOSPHONATE'>2PO</scene></td></tr> |
| - | [ | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | [[ | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2inv|2inv]]</td></tr> |
| - | [ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inulin_fructotransferase_(DFA-III-forming) Inulin fructotransferase (DFA-III-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.18 4.2.2.18] </span></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2inu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2inu OCA], [http://pdbe.org/2inu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2inu RCSB], [http://www.ebi.ac.uk/pdbsum/2inu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2inu ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/in/2inu_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2inu ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Inulin fructotransferase (IFTase), a member of glycoside hydrolase family 91, catalyzes depolymerization of beta-2,1-fructans inulin by successively removing the terminal difructosaccharide units as cyclic anhydrides via intramolecular fructosyl transfer. The crystal structures of IFTase and its substrate-bound complex reveal that IFTase is a trimeric enzyme, and each monomer folds into a right-handed parallel beta-helix. Despite variation in the number and conformation of its beta-strands, the IFTase beta-helix has a structure that is largely reminiscent of other beta-helix structures but is unprecedented in that trimerization is a prerequisite for catalytic activity, and the active site is located at the monomer-monomer interface. Results from crystallographic studies and site-directed mutagenesis provide a structural basis for the exolytic-type activity of IFTase and a functional resemblance to inverting-type glycosyltransferases. | ||
| - | + | Structural and functional insights into intramolecular fructosyl transfer by inulin fructotransferase.,Jung WS, Hong CK, Lee S, Kim CS, Kim SJ, Kim SI, Rhee S J Biol Chem. 2007 Mar 16;282(11):8414-23. Epub 2006 Dec 27. PMID:17192265<ref>PMID:17192265</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2inu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus sp. snu-7]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jung, W S]] | ||
| + | [[Category: Rhee, S]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Right-handed parallel beta-helix]] | ||
Current revision
Crystal structure of Inulin fructotransferase in the absence of substrate
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