View source for 9j4l


==Crystal structure of GH9l Inulin fructotransferases (IFTase)==
<StructureSection load='9j4l' size='340' side='right'caption='[[9j4l]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9j4l]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenarthrobacter_aurescens Paenarthrobacter aurescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9J4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9J4L 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]] 2.15&#8491;</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=9j4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9j4l OCA], [https://pdbe.org/9j4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9j4l RCSB], [https://www.ebi.ac.uk/pdbsum/9j4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9j4l ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F8QV43_PAEAU F8QV43_PAEAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycoside hydrolase family 91 (GH91) inulin fructotransferase (IFTases) enables biotransformation of fructans into sugar substitutes for dietary intervention in metabolic syndrome. However, the catalytic mechanism underlying the sequential biodegradation of inulin remains unelusive during the biotranformation of fructans. Herein we present the crystal structures of IFTase from Arthrobacter aurescens SK 8.001 in apo form and in complexes with kestose, nystose, or fructosyl nystose, respectively. Two kinds of conserved noncatalytic binding regions are first identified for IFTase-inulin interactions. The conserved interactions of substrates were revealed in the catalytic center that only contained a catalytic residue E205. A switching scaffold was comprised of D194 and Q217 in the catalytic channel, which served as the catalytic transition stabilizer through side chain displacement in the cycling of substrate sliding in/out the catalytic pocket. Such features in GH91 contribute to the catalytic model for consecutive cutting of substrate chain as well as product release in IFTase, and thus might be extended to other exo-active enzymes with an enclosed bottom of catalytic pocket. The study expands the current general catalytic principle in enzyme-substrate complexes and shed light on the rational design of IFTase for fructan biotransformation.

Elucidation of the mechanism underlying the sequential catalysis of inulin by fructotransferase.,Chen G, Wang ZX, Yang Y, Li Y, Zhang T, Ouyang S, Zhang L, Chen Y, Ruan X, Miao M Int J Biol Macromol. 2024 Aug 2:134446. doi: 10.1016/j.ijbiomac.2024.134446. PMID:39098696<ref>PMID:39098696</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9j4l" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paenarthrobacter aurescens]]
[[Category: Chen G]]
[[Category: Chen Y]]
[[Category: Li YG]]
[[Category: Miao M]]
[[Category: Ouyang SY]]
[[Category: Ruan XL]]
[[Category: Wang ZX]]
[[Category: Yang YQ]]
[[Category: Zhang L]]
[[Category: Zhang T]]