1RH9

Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)

1RH9 の概要

• エントリーDOI: 10.2210/pdb1rh9/pdb
• 関連するPDBエントリー: 1BQC 1QNP
• 分子名称: endo-beta-mannanase (1 entity in total)
• 機能のキーワード: endo-beta-mannase, retaining, glycoside hydrolase family 5, mannan, hydrolase
• 由来する生物種: Solanum lycopersicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42435.91

構造登録者

Oakley, A.J.,Bourgault, R.,Bewley, J.D.,Wilce, M.C.J. (登録日: 2003-11-14, 公開日: 2005-04-19, 最終更新日: 2024-10-30)

主引用文献

Bourgault, R.,Oakley, A.J.,Bewley, J.D.,Wilce, M.C.
Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit.
Protein Sci., 14:1233-1241, 2005

PubMed Abstract: The three-dimensional crystal structure of tomato (Lycopersicon esculentum) beta-mannanase 4a (LeMAN4a) has been determined to 1.5 A resolution. The enzyme adopts the (beta/alpha)(8) fold common to the members of glycohydrolase family GH5. The structure is comparable with those of the homologous Trichoderma reesei and Thermomonospora fusca beta-mannanases: There is a conserved three-stranded beta-sheet located near the N terminus that stacks against the central beta-barrel at the end opposite the active site. Three noncanonical beta-helices surround the active site. Similar helices are found in T. reesei but not T. fusca beta-mannanase. By analogy with other beta-mannanases, the catalytic acid/base residue is E204 and the nucleophile residue is E318. The active site cleft of L. esculentum beta-mannanase most closely resembles that of the T. reesei isozyme. A model of substrate binding in LeMAN4a is proposed in which the mannosyl residue occupying the -1 subsite of the enzyme adopts the (1)S(5) skew-boat conformation.

PubMed: 15840830
DOI: 10.1110/ps.041260905

実験手法

X-RAY DIFFRACTION (1.5 Å)