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New page: left|200px<br /><applet load="2uwb" size="350" color="white" frame="true" align="right" spinBox="true" caption="2uwb, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:2uwb.gif|left|200px]]<br /><applet load="2uwb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2uwb, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF THE NASTURTIUM SEEDLING MUTANT XYLOGLUCANASE ISOFORM NXG1-DELTA-YNIIG'''<br />


==Overview==
==Crystal structure of the Nasturtium seedling mutant xyloglucanase isoform NXG1-delta-YNIIG==
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.
<StructureSection load='2uwb' size='340' side='right'caption='[[2uwb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2uwb]] 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=2UWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UWB 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&#8491;</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=2uwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwb OCA], [https://pdbe.org/2uwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uwb RCSB], [https://www.ebi.ac.uk/pdbsum/2uwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uwb 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/2uwb_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=2uwb 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.


==About this Structure==
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>
2UWB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tropaeolum_majus Tropaeolum majus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWB OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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 8;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17557806 17557806]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 2uwb" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tropaeolum majus]]
[[Category: Tropaeolum majus]]
[[Category: Baumann, M.J.]]
[[Category: Baumann MJ]]
[[Category: Brumer, H.]]
[[Category: Brumer H]]
[[Category: Czjzek, M.]]
[[Category: Czjzek M]]
[[Category: Eklof, J.]]
[[Category: Eklof J]]
[[Category: Kallasa, A.]]
[[Category: Kallasa A]]
[[Category: Michel, G.]]
[[Category: Michel G]]
[[Category: Teeri, T.T.]]
[[Category: Teeri TT]]
[[Category: family gh16]]
[[Category: glycosidase]]
[[Category: glycoside hydrolase]]
[[Category: hydrolase]]
[[Category: loop mutant nxg1- yniig]]
[[Category: tropaeolum majus xyloglucanase]]
[[Category: xyloglucan-endo-transferase]]
 
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