2uwc
From Proteopedia
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- | [[Image:2uwc.gif|left|200px]] | ||
- | + | ==Crystal structure of Nasturtium xyloglucan hydrolase isoform NXG2== | |
- | + | <StructureSection load='2uwc' size='340' side='right'caption='[[2uwc]], [[Resolution|resolution]] 2.30Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2uwc]] 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=2UWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UWC FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=2uwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwc OCA], [https://pdbe.org/2uwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uwc RCSB], [https://www.ebi.ac.uk/pdbsum/2uwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uwc ProSAT]</span></td></tr> | |
- | + | </table> | |
- | + | == 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] | |
- | + | == Evolutionary Conservation == | |
- | + | [[Image:Consurf_key_small.gif|200px|right]] | |
- | + | Check<jmol> | |
- | + | <jmolCheckbox> | |
- | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uw/2uwc_consurf.spt"</scriptWhenChecked> | |
- | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2uwc ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
High-resolution, three-dimensional structures of the archetypal glycoside hydrolase family 16 (GH16) endo-xyloglucanases Tm-NXG1 and Tm-NXG2 from nasturtium (Tropaeolum majus) have been solved by x-ray crystallography. Key structural features that modulate the relative rates of substrate hydrolysis to transglycosylation in the GH16 xyloglucan-active enzymes were identified by structure-function studies of the recombinantly expressed enzymes in comparison with data for the strict xyloglucan endo-transglycosylase Ptt-XET16-34 from hybrid aspen (Populus tremula x Populus tremuloides). Production of the loop deletion variant Tm-NXG1-DeltaYNIIG yielded an enzyme that was structurally similar to Ptt-XET16-34 and had a greatly increased transglycosylation:hydrolysis ratio. Comprehensive bioinformatic analyses of XTH gene products, together with detailed kinetic data, strongly suggest that xyloglucanase activity has evolved as a gain of function in an ancestral GH16 XET to meet specific biological requirements during seed germination, fruit ripening, and rapid wall expansion. | High-resolution, three-dimensional structures of the archetypal glycoside hydrolase family 16 (GH16) endo-xyloglucanases Tm-NXG1 and Tm-NXG2 from nasturtium (Tropaeolum majus) have been solved by x-ray crystallography. Key structural features that modulate the relative rates of substrate hydrolysis to transglycosylation in the GH16 xyloglucan-active enzymes were identified by structure-function studies of the recombinantly expressed enzymes in comparison with data for the strict xyloglucan endo-transglycosylase Ptt-XET16-34 from hybrid aspen (Populus tremula x Populus tremuloides). Production of the loop deletion variant Tm-NXG1-DeltaYNIIG yielded an enzyme that was structurally similar to Ptt-XET16-34 and had a greatly increased transglycosylation:hydrolysis ratio. Comprehensive bioinformatic analyses of XTH gene products, together with detailed kinetic data, strongly suggest that xyloglucanase activity has evolved as a gain of function in an ancestral GH16 XET to meet specific biological requirements during seed germination, fruit ripening, and rapid wall expansion. | ||
- | + | Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism.,Baumann MJ, Eklof JM, Michel G, Kallas AM, Teeri TT, Czjzek M, Brumer H 3rd Plant Cell. 2007 Jun;19(6):1947-63. Epub 2007 Jun 8. PMID:17557806<ref>PMID:17557806</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | [[Category: | + | <div class="pdbe-citations 2uwc" style="background-color:#fffaf0;"></div> |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Tropaeolum majus]] | [[Category: Tropaeolum majus]] | ||
- | [[Category: Baumann | + | [[Category: Baumann MJ]] |
- | [[Category: Brumer | + | [[Category: Brumer H]] |
- | [[Category: Czjzek | + | [[Category: Czjzek M]] |
- | [[Category: Eklof | + | [[Category: Eklof JM]] |
- | [[Category: Kallas | + | [[Category: Kallas A]] |
- | [[Category: Michel | + | [[Category: Michel G]] |
- | [[Category: Teeri | + | [[Category: Teeri TT]] |
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Current revision
Crystal structure of Nasturtium xyloglucan hydrolase isoform NXG2
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Categories: Large Structures | Tropaeolum majus | Baumann MJ | Brumer H | Czjzek M | Eklof JM | Kallas A | Michel G | Teeri TT