2qqv

From Proteopedia

(Difference between revisions)

Revision as of 11:27, 5 September 2018

Crystal structure of a cell-wall invertase (E203A) from Arabidopsis thaliana in complex with sucrose

Structural highlights

2qqv is a 1 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	2ac1, 2oxb, 2qqw
Gene:	ATBFRUCT1 (ARATH)
Activity:	Beta-fructofuranosidase, with EC number 3.2.1.26
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 plants, cell-wall invertases fulfil important roles in carbohydrate partitioning, growth, development and crop yield. In this study, we report on different X-ray crystal structures of Arabidopsis thaliana cell-wall invertase 1 (AtcwINV1) mutants with sucrose. These structures reveal a detailed view of sucrose binding in the active site of the wild-type AtcwINV1. Compared to related enzyme-sucrose complexes, important differences in the orientation of the glucose subunit could be observed. The structure of the E203Q AtcwINV1 mutant showed a complete new binding modus, whereas the D23A, E203A and D239A structures most likely represent the productive binding modus. Together with a hydrophobic zone formed by the conserved W20, W47 and W82, the residues N22, D23, R148, E203, D149 and D239 are necessary to create the ideal sucrose-binding pocket. D239 can interact directly with the glucose moiety of sucrose, whereas K242 has an indirect role in substrate stabilization. Most probably, K242 keeps D239 in a favourable position upon substrate binding. Unravelling the exact position of sucrose in plant cell-wall invertases is a necessary step towards the rational design of superior invertases to further increase crop yield and biomass production.

Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose.,Lammens W, Le Roy K, Van Laere A, Rabijns A, Van den Ende W J Mol Biol. 2008 Mar 21;377(2):378-85. Epub 2008 Jan 5. PMID:18258263^[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
↑ Lammens W, Le Roy K, Van Laere A, Rabijns A, Van den Ende W. Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose. J Mol Biol. 2008 Mar 21;377(2):378-85. Epub 2008 Jan 5. PMID:18258263 doi:10.1016/j.jmb.2007.12.074

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/2qqv"

@@ Line 1: / Line 1: @@
 ==Crystal structure of a cell-wall invertase (E203A) from Arabidopsis thaliana in complex with sucrose==
 <StructureSection load='2qqv' size='340' side='right' caption='[[2qqv]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2qqv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QQV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ac1|2ac1]], [[2oxb|2oxb]], [[2qqw|2qqw]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATBFRUCT1 ([http://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'>[http://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqv OCA], [http://pdbe.org/2qqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qqv RCSB], [http://www.ebi.ac.uk/pdbsum/2qqv PDBsum]</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=2qqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqv OCA], [http://pdbe.org/2qqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qqv RCSB], [http://www.ebi.ac.uk/pdbsum/2qqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qqv ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qq/2qqv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qq/2qqv_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2qqv

From Proteopedia

Revision as of 11:27, 5 September 2018

Crystal structure of a cell-wall invertase (E203A) 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?)

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