Purification and crystallization of a trimodular complex comprising the type II cohesin-dockerin interaction from the cellulosome of Clostridium thermocellum.
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 A. The asymmetric unit contains one molecule of the protein complex and native and selenomethionine-derivative crystals diffracted to 2.1 and 2.0 A, respectively.
Adams
Jarrett J
JJ
Department of Biochemistry, Queen's University, Kingston, ON, K7L 3N6, Canada.
Pal
Gour
G
Yam
Katherine
K
Spencer
Holly L
HL
Jia
Zongchao
Z
Smith
Steven P
SP
D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002482:Cellulose / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone / Q000302:isolation & purification / Q000378:metabolism*; D048013:Acetivibrio thermocellus / Q000378:metabolism*; D003460:Crystallization; D009097:Multienzyme Complexes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D009687:Nuclear Proteins / Q000302:isolation & purification / Q000378:metabolism*; D014961:X-Ray Diffraction; D000097722:Cohesins
D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D002482:Cellulose; D002868:Chromosomal Proteins, Non-Histone; D009097:Multienzyme Complexes; D009687:Nuclear Proteins; D000097722:Cohesins