2UWC

Crystal structure of Nasturtium xyloglucan hydrolase isoform NXG2

2UWC の概要

• エントリーDOI: 10.2210/pdb2uwc/pdb
• 関連するPDBエントリー: 2UWB
• 分子名称: CELLULASE (2 entities in total)
• 機能のキーワード: tropaeolum majus, xyloglucan hydrolase, xyloglucan-endo-transferase, hydrolase, glycosidase, family gh16, isoform nxg2
• 由来する生物種: TROPAEOLUM MAJUS (NASTURTIUM)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61832.17

構造登録者

Baumann, M.J.,Eklof, J.M.,Michel, G.,Kallas, A.,Teeri, T.T.,Brumer, H.,Czjzek, M. (登録日: 2007-03-20, 公開日: 2007-06-26, 最終更新日: 2024-11-13)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.3 Å)