2uwc
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwc OCA], [http://www.ebi.ac.uk/pdbsum/2uwc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2uwc RCSB]</span> | ||
}} | }} | ||
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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 Mon Mar 31 05:05:24 2008'' |
Revision as of 02:05, 31 March 2008
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, resolution 2.30Å | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
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
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