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2UWB

Crystal structure of the Nasturtium seedling mutant xyloglucanase isoform NXG1-delta-YNIIG

Summary for 2UWB
Entry DOI10.2210/pdb2uwb/pdb
Related2UWA 2UWC
DescriptorCELLULASE (2 entities in total)
Functional Keywordsxyloglucan-endo-transferase, glycoside hydrolase, loop mutant nxg1- yniig, hydrolase, glycosidase, family gh16, tropaeolum majus xyloglucanase
Biological sourceTROPAEOLUM MAJUS (NASTURTIUM)
Total number of polymer chains2
Total formula weight60909.15
Authors
Baumann, M.J.,Eklof, J.,Michel, G.,Kallasa, A.,Teeri, T.T.,Brumer, H.,Czjzek, M. (deposition date: 2007-03-20, release date: 2007-06-26, Last modification date: 2024-11-13)
Primary citationBaumann, M.J.,Eklof, J.,Michel, G.,Kallasa, A.,Teeri, T.T.,Czjzek, M.,Brumer, H.
Structural Evidence for the Evolution of Xyloglucanase Activity from Xyloglucan Endo-Transglycosylases: Biological Implications for Cell Wall Metabolism.
Plant Cell, 19:1947-, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17557806
DOI: 10.1105/TPC.107.051391
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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数据于2025-10-08公开中

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