2qqu: Difference between revisions
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==Crystal structure of a cell-wall invertase (D239A) from Arabidopsis thaliana in complex with sucrose== | ==Crystal structure of a cell-wall invertase (D239A) from Arabidopsis thaliana in complex with sucrose== | ||
<StructureSection load='2qqu' size='340' side='right' caption='[[2qqu]], [[Resolution|resolution]] 2.84Å' scene=''> | <StructureSection load='2qqu' size='340' side='right'caption='[[2qqu]], [[Resolution|resolution]] 2.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qqu]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2qqu]] 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=2QQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QQU FirstGlance]. <br> | ||
</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= | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84Å</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=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=PRD_900003:sucrose'>PRD_900003</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2qqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqu OCA], [https://pdbe.org/2qqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qqu RCSB], [https://www.ebi.ac.uk/pdbsum/2qqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qqu ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Lammens W]] | |||
[[Category: Le Roy K]] | |||
[[Category: Lammens | [[Category: Rabijns A]] | ||
[[Category: | [[Category: Van Laere A]] | ||
[[Category: Van den Ende W]] | |||
[[Category: | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 14:39, 30 August 2023
Crystal structure of a cell-wall invertase (D239A) from Arabidopsis thaliana in complex with sucroseCrystal structure of a cell-wall invertase (D239A) from Arabidopsis thaliana in complex with sucrose
Structural highlights
FunctionINV1_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 PubMedIn 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. See AlsoReferences
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