|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='2vh9' size='340' side='right'caption='[[2vh9]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2vh9' size='340' side='right'caption='[[2vh9]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vh9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Common_nasturtium Common nasturtium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VH9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vh9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tropaeolum_majus Tropaeolum majus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VH9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2uwa|2uwa]], [[2uwb|2uwb]], [[2uwc|2uwc]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</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=2vh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vh9 OCA], [https://pdbe.org/2vh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vh9 RCSB], [https://www.ebi.ac.uk/pdbsum/2vh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vh9 ProSAT]</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=2vh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vh9 OCA], [https://pdbe.org/2vh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vh9 RCSB], [https://www.ebi.ac.uk/pdbsum/2vh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vh9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q07524_TROMA Q07524_TROMA]] Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues.[RuleBase:RU361120]
| + | [https://www.uniprot.org/uniprot/Q07524_TROMA Q07524_TROMA] Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues.[RuleBase:RU361120] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Common nasturtium]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baumann, M J]] | + | [[Category: Tropaeolum majus]] |
| - | [[Category: Brumer, H]] | + | [[Category: Baumann MJ]] |
| - | [[Category: Czjzek, M]] | + | [[Category: Brumer H]] |
| - | [[Category: Eklof, J M]] | + | [[Category: Czjzek M]] |
| - | [[Category: Mark, P]] | + | [[Category: Eklof JM]] |
| - | [[Category: Michel, G]] | + | [[Category: Mark P]] |
| - | [[Category: Family gh16]]
| + | [[Category: Michel G]] |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Loop mutant nxg1-yniig]]
| + | |
| - | [[Category: Substrate complex]]
| + | |
| - | [[Category: Tropaeolum majus xyloglucanase]]
| + | |
| - | [[Category: Xllg oligosaccharide]]
| + | |
| Structural highlights
2vh9 is a 2 chain structure with sequence from Tropaeolum majus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.1Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q07524_TROMA Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues.[RuleBase:RU361120]
Publication Abstract from PubMed
Reorganization and degradation of the wall crosslinking and seed storage polysaccharide xyloglucan by glycoside hydrolase family 16 (GH16) endo-transglycosylases and hydrolases are crucial to the growth of the majority of land plants, affecting processes as diverse as germination, morphogenesis, and fruit ripening. A high-resolution, three-dimensional structure of a nasturtium (Tropaeolum majus) endo-xyloglucanase loop mutant, TmNXG1-DeltaYNIIG, with an oligosaccharide product bound in the negative active-site subsites, has been solved by X-ray crystallography. Comparison of this novel complex to that of the strict xyloglucan endo-transglycosylase PttXET16-34 from hybrid aspen (Populus tremula x tremuloides), previously solved with a xylogluco-oligosaccharide bound in the positive subsites, highlighted key protein structures that affect the disparate catalytic activities displayed by these closely related enzymes. Combination of these "partial" active-site complexes through molecular dynamics simulations in water allowed modeling of wild-type TmNXG1, TmNXG1-DeltaYNIIG, and wild-type PttXET16-34 in complex with a xyloglucan octadecasaccharide spanning the entire catalytic cleft. A comprehensive analysis of these full-length complexes underscored the importance of various loops lining the active site. Subtle differences leading to a tighter hydrogen bonding pattern on the negative (glycosyl donor) binding subsites, together with loop flexibility on the positive (glycosyl acceptor) binding subsites appear to favor hydrolysis over transglycosylation in GH16 xyloglucan-active enzymes. Proteins 2009. (c) 2008 Wiley-Liss, Inc.
Analysis of nasturtium TmNXG1 complexes by crystallography and molecular dynamics provides detailed insight into substrate recognition by family GH16 xyloglucan endo-transglycosylases and endo-hydrolases.,Mark P, Baumann MJ, Eklof JM, Gullfot F, Michel G, Kallas AM, Teeri TT, Brumer H, Czjzek M Proteins. 2008 Oct 3. PMID:19004021[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mark P, Baumann MJ, Eklof JM, Gullfot F, Michel G, Kallas AM, Teeri TT, Brumer H, Czjzek M. Analysis of nasturtium TmNXG1 complexes by crystallography and molecular dynamics provides detailed insight into substrate recognition by family GH16 xyloglucan endo-transglycosylases and endo-hydrolases. Proteins. 2008 Oct 3. PMID:19004021 doi:10.1002/prot.22291
|
