1ANU

COHESIN-2 DOMAIN OF THE CELLULOSOME FROM CLOSTRIDIUM THERMOCELLUM

1ANU の概要

• エントリーDOI: 10.2210/pdb1anu/pdb
• 分子名称: COHESIN-2 (2 entities in total)
• 機能のキーワード: cohesin, scaffolding, cellulose digestion, beta sandwich, thermophile
• 由来する生物種: Clostridium thermocellum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14752.65

構造登録者

Shimon, L.J.W.,Yaron, S.,Shoham, Y.,Lamed, R.,Morag, E.,Bayer, E.A.,Frolow, F. (登録日: 1996-07-19, 公開日: 1997-07-23, 最終更新日: 2024-02-07)

主引用文献

Shimon, L.J.,Bayer, E.A.,Morag, E.,Lamed, R.,Yaron, S.,Shoham, Y.,Frolow, F.
A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly.
Structure, 5:381-390, 1997

PubMed Abstract: The scaffoldin component of the cellulolytic bacterium Clostridium thermocellum is a non-hydrolytic protein which organizes the hydrolytic enzymes in a large complex, called the cellulosome. Scaffoldin comprises a series of functional domains, amongst which is a single cellulose-binding domain and nine cohesin domains which are responsible for integrating the individual enzymatic subunits into the complex. The cohesin domains are highly conserved in their primary amino acid sequences. These domains interact with a complementary domain, termed the dockerin domain, one of which is located on each enzymatic subunit. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The determination of structural information about the cohesin domain will provide insights into cellulosome assembly and activity.

PubMed: 9083107
DOI: 10.1016/S0969-2126(97)00195-0

実験手法

X-RAY DIFFRACTION (2.15 Å)