2inu

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(New page: 200px<br /><applet load="2inu" size="350" color="white" frame="true" align="right" spinBox="true" caption="2inu, resolution 1.8&Aring;" /> '''Crystal structure of ...)
Current revision (05:17, 17 October 2024) (edit) (undo)
 
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[[Image:2inu.jpg|left|200px]]<br /><applet load="2inu" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2inu, resolution 1.8&Aring;" />
 
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'''Crystal structure of inulin fructotransferase in the absence of substrate'''<br />
 
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==About this Structure==
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==Crystal structure of Inulin fructotransferase in the absence of substrate==
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2INU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp._snu-7 Bacillus sp. snu-7] with <scene name='pdbligand=2PO:'>2PO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2INU OCA].
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<StructureSection load='2inu' size='340' side='right'caption='[[2inu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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[[Category: Bacillus sp. snu-7]]
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== Structural highlights ==
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[[Category: Inulin fructotransferase (DFA-III-forming)]]
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<table><tr><td colspan='2'>[[2inu]] is a 3 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2INU FirstGlance]. <br>
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[[Category: Single protein]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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[[Category: Jung, W.S.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PO:PHOSPHONATE'>2PO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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[[Category: Rhee, S.]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2inu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2inu OCA], [https://pdbe.org/2inu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2inu RCSB], [https://www.ebi.ac.uk/pdbsum/2inu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2inu ProSAT]</span></td></tr>
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[[Category: 2PO]]
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</table>
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[[Category: right-handed parallel beta-helix]]
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== Function ==
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[https://www.uniprot.org/uniprot/Q3SAG3_9BACI Q3SAG3_9BACI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/in/2inu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:44:10 2008''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2inu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus sp. snu-7]]
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[[Category: Large Structures]]
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[[Category: Jung WS]]
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[[Category: Rhee S]]

Current revision

Crystal structure of Inulin fructotransferase in the absence of substrate

PDB ID 2inu

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