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2oxb

From Proteopedia

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Crystal structure of a cell-wall invertase (E203Q) from Arabidopsis thaliana in complex with sucrose

Structural highlights

2oxb is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

INV1_ARATH Beta-fructofuranosidase that can use sucrose and 1-kestose, and, to a lower extent, neokestose and levan, as substrates, but not inuline.^[1] ^[2]

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

In the present study, we report on the X-ray crystallographic structure of a GH32 invertase mutant, (i.e., the Arabidopsis thaliana cell-wall invertase 1-E203Q, AtcwINV1-mutant) in complex with sucrose. This structure was solved to reveal the features of sugar binding in the catalytic pocket. However, as demonstrated by the X-ray structure the sugar binding and the catalytic pocket arrangement is significantly altered as compared with what was expected based on previous X-ray structures on GH-J clan enzymes. We performed a series of docking and molecular dynamics simulations on various derivatives of AtcwINV1 to reveal the reasons behind this modified sugar binding. Our results demonstrate that the E203Q mutation introduced into the catalytic pocket triggers conformational changes that alter the wild type substrate binding. In addition, this study also reveals the putative productive sucrose binding modus in the wild type enzyme. Proteins 2007. (c) 2007 Wiley-Liss, Inc.

An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study.,Matrai J, Lammens W, Jonckheer A, Le Roy K, Rabijns A, Van den Ende W, De Maeyer M Proteins. 2007 Oct 26;. PMID:17963237^[3]

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

References

↑ Matrai J, Lammens W, Jonckheer A, Le Roy K, Rabijns A, Van den Ende W, De Maeyer M. An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study. Proteins. 2007 Oct 26;. PMID:17963237 doi:10.1002/prot.21700
↑ Le Roy K, Lammens W, Verhaest M, De Coninck B, Rabijns A, Van Laere A, Van den Ende W. Unraveling the difference between invertases and fructan exohydrolases: a single amino acid (Asp-239) substitution transforms Arabidopsis cell wall invertase1 into a fructan 1-exohydrolase. Plant Physiol. 2007 Nov;145(3):616-25. Epub 2007 Sep 14. PMID:17873089 doi:pp.107.105049
↑ Matrai J, Lammens W, Jonckheer A, Le Roy K, Rabijns A, Van den Ende W, De Maeyer M. An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study. Proteins. 2007 Oct 26;. PMID:17963237 doi:10.1002/prot.21700

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2oxb"

@@ Line 3: / Line 3: @@
 <StructureSection load='2oxb' size='340' side='right'caption='[[2oxb]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2oxb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OXB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2oxb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OXB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ac1|2ac1]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATBFRUCT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26] </span></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=2oxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxb OCA], [https://pdbe.org/2oxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oxb RCSB], [https://www.ebi.ac.uk/pdbsum/2oxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oxb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/INV1_ARATH INV1_ARATH]] Beta-fructofuranosidase that can use sucrose and 1-kestose, and, to a lower extent, neokestose and levan, as substrates, but not inuline.<ref>PMID:17963237</ref> <ref>PMID:17873089</ref>
+[https://www.uniprot.org/uniprot/INV1_ARATH INV1_ARATH] Beta-fructofuranosidase that can use sucrose and 1-kestose, and, to a lower extent, neokestose and levan, as substrates, but not inuline.<ref>PMID:17963237</ref> <ref>PMID:17873089</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 38: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Beta-fructofuranosidase]]
 [[Category: Large Structures]]
-[[Category: Ende, W Van den]]
+[[Category: Lammens W]]
-[[Category: Laere, A Van]]
+[[Category: Le Roy K]]
-[[Category: Lammens, W]]
+[[Category: Rabijns A]]
-[[Category: Rabijns, A]]
+[[Category: Van Laere A]]
-[[Category: Roy, K Le]]
+[[Category: Van den Ende W]]
-[[Category: Hydrolase]]

2oxb

From Proteopedia

Current revision

Crystal structure of a cell-wall invertase (E203Q) from Arabidopsis thaliana in complex with sucrose

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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