1WVU

Crystal structure of chitinase C from Streptomyces griseus HUT6037

1WVU の概要

• エントリーDOI: 10.2210/pdb1wvu/pdb
• 関連するPDBエントリー: 1WVV
• 分子名称: chitinase C, CHLORIDE ION (3 entities in total)
• 機能のキーワード: family 19 chitinase, whole structure, hydrolase
• 由来する生物種: Streptomyces griseus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57455.23

構造登録者

Kezuka, Y.,Watanabe, T.,Nonaka, T. (登録日: 2004-12-27, 公開日: 2005-12-27, 最終更新日: 2024-10-16)

主引用文献

Kezuka, Y.,Ohishi, M.,Itoh, Y.,Watanabe, J.,Mitsutomi, M.,Watanabe, T.,Nonaka, T.
Structural Studies of a Two-domain Chitinase from Streptomyces griseus HUT6037
J.Mol.Biol., 358:472-484, 2006

PubMed Abstract: Chitinase C (ChiC) from Streptomyces griseus HUT6037 was the first glycoside hydrolase family 19 chitinase that was found in an organism other than higher plants. An N-terminal chitin-binding domain and a C-terminal catalytic domain connected by a linker peptide constitute ChiC. We determined the crystal structure of full-length ChiC, which is the only representative of the two-domain chitinases in the family. The catalytic domain has an alpha-helix-rich fold with a deep cleft containing a catalytic site, and lacks three loops on the domain surface compared with the catalytic domain of plant chitinases. The chitin-binding domain is an all-beta protein with two tryptophan residues (Trp59 and Trp60) aligned on the surface. We suggest the binding mechanism of tri-N-acetylchitotriose onto the chitin-binding domain on the basis of molecular dynamics (MD) simulations. In this mechanism, the ligand molecule binds well on the surface-exposed binding site through two stacking interactions and two hydrogen bonds and only Trp59 and Trp60 are involved in the binding. Furthermore, the flexibility of the Trp60 side-chain, which may be involved in adjusting the binding surface to fit the surface of crystalline chitin by the rotation of chi2 angle, is shown.

PubMed: 16516924
DOI: 10.1016/j.jmb.2006.02.013

実験手法

X-RAY DIFFRACTION (2.45 Å)