4hoz: Difference between revisions
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The | ==The crystal structure of isomaltulose synthase mutant D241A from Erwinia rhapontici NX5 in complex with D-glucose== | ||
<StructureSection load='4hoz' size='340' side='right'caption='[[4hoz]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hoz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Erwinia_rhapontici Erwinia rhapontici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HOZ 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4hoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hoz OCA], [https://pdbe.org/4hoz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hoz RCSB], [https://www.ebi.ac.uk/pdbsum/4hoz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hoz ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D9MPF2_ERWRD D9MPF2_ERWRD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sucrose isomerase NX-5 from Erwiniarhapontici efficiently catalyzes the isomerization of sucrose to isomaltulose (main product) and trehalulose (by-product). To investigate the molecular mechanism controlling sucrose isomer formation, we determined the crystal structures of native NX-5 and its mutant complexes E295Q/sucrose and D241A/glucose at 1.70 A, 1.70 A and 2.00 A, respectively. The overall structure and active site architecture of NX-5 resemble those of other reported sucrose isomerases. Strikingly, the substrate binding mode of NX-5 is also similar to that of trehalulose synthase from Pseudomonasmesoacidophila MX-45 (MutB). Detailed structural analysis revealed the catalytic RXDRX motif and the adjacent 10-residue loop of NX-5 and isomaltulose synthase PalI from Klebsiella sp. LX3 adopt a distinct orientation from those of trehalulose synthases. Mutations of the loop region of NX-5 resulted in significant changes of the product ratio between isomaltulose and trehalulose. The molecular dynamics simulation data supported the product specificity of NX-5 towards isomaltulose and the role of the loop(330-339) in NX-5 catalysis. This work should prove useful for the engineering of sucrose isomerase for industrial carbohydrate biotransformations. | |||
The Structural Basis of Erwinia rhapontici Isomaltulose Synthase.,Xu Z, Li S, Li J, Li Y, Feng X, Wang R, Xu H, Zhou J PLoS One. 2013 Sep 19;8(9):e74788. doi: 10.1371/journal.pone.0074788. PMID:24069347<ref>PMID:24069347</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hoz" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Trehalulose synthase|Trehalulose synthase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Erwinia rhapontici]] | |||
[[Category: Large Structures]] | |||
[[Category: Li S]] | |||
[[Category: Xu H]] | |||
[[Category: Xu Z]] | |||
[[Category: Zhou J]] | |||