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| [[Image:2uwc.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2uwc| PDB=2uwc | SCENE= }} | | {{STRUCTURE_2uwc| PDB=2uwc | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF NASTURTIUM XYLOGLUCAN HYDROLASE ISOFORM NXG2'''
| | ===CRYSTAL STRUCTURE OF NASTURTIUM XYLOGLUCAN HYDROLASE ISOFORM NXG2=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17557806}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17557806 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17557806}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Xyloglucan hydrolase]] | | [[Category: Xyloglucan hydrolase]] |
| [[Category: Xyloglucan-endo-transferase]] | | [[Category: Xyloglucan-endo-transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:39:19 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:42:18 2008'' |
