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

Journal Article · Sat Jan 01 04:00:00 EST 2005 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309104025837· OSTI ID:22356086

Adams, Jarrett J.; Pal, Gour; Yam, Katherine; Spencer, Holly L. ^[1]; Jia, Zongchao

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1. Department of Biochemistry, Queen’s University, Kingston, ON, K7L 3N6 (Canada)

A trimodular complex comprising the type II cohesin–dockerin interaction from the cellulosome of C. thermocellum has been purified and crystallized by the hanging-drop vapour-diffusion method. A native crystal and a selenomethionine derivative have been analyzed using X-ray diffraction. 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{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 45.21, b = 52.34, c = 154.69 Å. The asymmetric unit contains one molecule of the protein complex and native and selenomethionine-derivative crystals diffracted to 2.1 and 2.0 Å, respectively.

• OSTI ID: 22356086
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 1 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
AFFINITY
CALCIUM
CELLULOSE
CRYSTALLIZATION
CRYSTALS
DIFFUSION
INTERACTIONS
MOLECULES
SPACE GROUPS
SURFACES
X-RAY DIFFRACTION