2inu: Difference between revisions

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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 1.8&Aring;" />
'''Crystal structure of inulin fructotransferase in the absence of substrate'''<br />


==About this Structure==
==Crystal structure of Inulin fructotransferase in the absence of substrate==
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].  
<StructureSection load='2inu' size='340' side='right'caption='[[2inu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q3SAG3_9BACI Q3SAG3_9BACI]
== 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/initialview03.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&reg;/PubMed&reg;, 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: Bacillus sp. snu-7]]
[[Category: Inulin fructotransferase (DFA-III-forming)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Jung WS]]
[[Category: Jung, W S.]]
[[Category: Rhee S]]
[[Category: Rhee, S.]]
[[Category: 2PO]]
[[Category: right-handed parallel beta-helix]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:54:28 2008''

Latest revision as of 05:17, 17 October 2024

Crystal structure of Inulin fructotransferase in the absence of substrate

2inu, resolution 1.80Å

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