Purification and crystallization of a trimodular complex comprising the type II cohesin-dockerin interaction from the cellulosome of Clostridium thermocellum

被引：7

作者：

Adams, JJ

Pal, G

Yam, K

Spencer, HL

Jia, Z

Smith, SP ^{[1
]}

机构：

[1] Queens Univ, Dept Biochem, Kingston, ON K7L 3N6, Canada

[2] Queens Univ, Prot Funct Discovery Grp, Kingston, ON K7L 3N6, Canada

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷

关键词：

D O I：

10.1107/S1744309104025837

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The high-affinity calcium-mediated type II cohesin-dockerin interaction is responsible for the attachment of the multi-enzyme cellulose-degrading complex, termed the cellulosome, to the cell surface of the thermophilic anaerobe Clostridium thermocellum. A trimodular 40 kDa complex comprising the SdbA type II cohesin and the the CipA type II dockerin-X module modular pair from the cellulosome of C. thermocellum has been crystallized. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 45.21, b = 52.34, c = 154.69 angstrom. The asymmetric unit contains one molecule of the protein complex and native and selenomethionine-derivative crystals diffracted to 2.1 and 2.0 angstrom, respectively.

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页码：46 / 48

页数：3

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