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==The crystal structure of isomaltulose synthase mutant D241A from Erwinia rhapontici NX5 in complex with D-glucose==
==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]] 2.00&Aring;' scene=''>
<StructureSection load='4hoz' size='340' side='right'caption='[[4hoz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4hoz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aplanobacter_rhaponticum"_(sic)_(millard_1924)_white_1936 "aplanobacter rhaponticum" (sic) (millard 1924) white 1936]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HOZ FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
</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&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4how|4how]], [[4hox|4hox]], [[4hp5|4hp5]], [[4hph|4hph]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PalI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=55212 "Aplanobacter rhaponticum" (sic) (Millard 1924) White 1936])</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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isomaltulose_synthase Isomaltulose synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.11 5.4.99.11] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hoz OCA], [http://pdbe.org/4hoz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hoz RCSB], [http://www.ebi.ac.uk/pdbsum/4hoz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hoz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D9MPF2_ERWRD D9MPF2_ERWRD]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4hoz" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4hoz" style="background-color:#fffaf0;"></div>
==See Also==
*[[Trehalulose synthase|Trehalulose synthase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Isomaltulose synthase]]
[[Category: Erwinia rhapontici]]
[[Category: Li, S]]
[[Category: Large Structures]]
[[Category: Xu, H]]
[[Category: Li S]]
[[Category: Xu, Z]]
[[Category: Xu H]]
[[Category: Zhou, J]]
[[Category: Xu Z]]
[[Category: Calcium binding]]
[[Category: Zhou J]]
[[Category: Hydrolase]]
[[Category: Isomerase]]
[[Category: Tim barrel]]

Latest revision as of 17:09, 8 November 2023

The crystal structure of isomaltulose synthase mutant D241A from Erwinia rhapontici NX5 in complex with D-glucoseThe crystal structure of isomaltulose synthase mutant D241A from Erwinia rhapontici NX5 in complex with D-glucose

Structural highlights

4hoz is a 1 chain structure with sequence from Erwinia rhapontici. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

D9MPF2_ERWRD

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Xu Z, Li S, Li J, Li Y, Feng X, Wang R, Xu H, Zhou J. The Structural Basis of Erwinia rhapontici Isomaltulose Synthase. PLoS One. 2013 Sep 19;8(9):e74788. doi: 10.1371/journal.pone.0074788. PMID:24069347 doi:http://dx.doi.org/10.1371/journal.pone.0074788

4hoz, resolution 2.00Å

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OCA