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| | <StructureSection load='2inv' size='340' side='right'caption='[[2inv]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2inv' size='340' side='right'caption='[[2inv]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2inv]] 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=2INV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2INV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2inv]] 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=2INV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2INV 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>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PO:PHOSPHONATE'>2PO</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2inu|2inu]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2inv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2inv OCA], [https://pdbe.org/2inv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2inv RCSB], [https://www.ebi.ac.uk/pdbsum/2inv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2inv ProSAT]</span></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=2inv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2inv OCA], [http://pdbe.org/2inv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2inv RCSB], [http://www.ebi.ac.uk/pdbsum/2inv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2inv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q3SAG3_9BACI Q3SAG3_9BACI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Bacillus sp. snu-7]] | | [[Category: Bacillus sp. snu-7]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jung, W S]] | + | [[Category: Jung WS]] |
| - | [[Category: Rhee, S]] | + | [[Category: Rhee S]] |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Protein-carbohydrate complex]]
| + | |
| - | [[Category: Right-handed parallel beta-helix]]
| + | |
| Structural highlights
Function
Q3SAG3_9BACI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jung WS, Hong CK, Lee S, Kim CS, Kim SJ, Kim SI, Rhee S. Structural and functional insights into intramolecular fructosyl transfer by inulin fructotransferase. J Biol Chem. 2007 Mar 16;282(11):8414-23. Epub 2006 Dec 27. PMID:17192265 doi:10.1074/jbc.M607143200
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