2UWC
Crystal structure of Nasturtium xyloglucan hydrolase isoform NXG2
Summary for 2UWC
| Entry DOI | 10.2210/pdb2uwc/pdb |
| Related | 2UWB |
| Descriptor | CELLULASE (2 entities in total) |
| Functional Keywords | tropaeolum majus, xyloglucan hydrolase, xyloglucan-endo-transferase, hydrolase, glycosidase, family gh16, isoform nxg2 |
| Biological source | TROPAEOLUM MAJUS (NASTURTIUM) |
| Total number of polymer chains | 2 |
| Total formula weight | 61832.17 |
| Authors | Baumann, M.J.,Eklof, J.M.,Michel, G.,Kallas, 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 citation | Baumann, M.J.,Eklof, J.M.,Michel, G.,Kallas, A.M.,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: 17557806DOI: 10.1105/TPC.107.051391 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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