2uwc
From Proteopedia
(New page: 200px<br /><applet load="2uwc" size="350" color="white" frame="true" align="right" spinBox="true" caption="2uwc, resolution 2.30Å" /> '''CRYSTAL STRUCTURE OF...) |
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==Overview== | ==Overview== | ||
| - | High-resolution, three-dimensional structures of the archetypal glycoside | + | 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structural | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17557806 17557806] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tropaeolum majus]] | [[Category: Tropaeolum majus]] | ||
| - | [[Category: Baumann, M | + | [[Category: Baumann, M J.]] |
[[Category: Brumer, H.]] | [[Category: Brumer, H.]] | ||
[[Category: Czjzek, M.]] | [[Category: Czjzek, M.]] | ||
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[[Category: Kallas, A.]] | [[Category: Kallas, A.]] | ||
[[Category: Michel, G.]] | [[Category: Michel, G.]] | ||
| - | [[Category: Teeri, T | + | [[Category: Teeri, T T.]] |
[[Category: family gh16]] | [[Category: family gh16]] | ||
[[Category: glycosidase]] | [[Category: glycosidase]] | ||
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[[Category: xyloglucan-endo-transferase]] | [[Category: xyloglucan-endo-transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:55 2008'' |
Revision as of 16:50, 21 February 2008
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CRYSTAL STRUCTURE OF NASTURTIUM XYLOGLUCAN HYDROLASE ISOFORM NXG2
Overview
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
2UWC is a Single protein structure of sequence from Tropaeolum majus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 18:50:55 2008
