2uwc
From Proteopedia
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| - | [[Image:2uwc.gif|left|200px]] | + | [[Image:2uwc.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF NASTURTIUM XYLOGLUCAN HYDROLASE ISOFORM NXG2''' | + | {{Structure |
| + | |PDB= 2uwc |SIZE=350|CAPTION= <scene name='initialview01'>2uwc</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF NASTURTIUM XYLOGLUCAN HYDROLASE ISOFORM NXG2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2UWC is a [ | + | 2UWC is a [[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=2UWC OCA]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/17557806 17557806] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tropaeolum majus]] | [[Category: Tropaeolum majus]] | ||
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[[Category: xyloglucan-endo-transferase]] | [[Category: xyloglucan-endo-transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:40:32 2008'' |
Revision as of 16:40, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 18:40:32 2008
