Mechanism of bacterial cell-surface attachment revealed by the structure of cellulosomal type II cohesin-dockerin complex

被引:84
作者
Adams, JJ
Pal, G
Jia, ZC
Smith, SP
机构
[1] Queens Univ, Dept Biochem, Kingston, ON K7L 3N6, Canada
[2] Queens Univ, Prot Funct Discovery Grp, Kingston, ON K7L 3N6, Canada
关键词
cellulose degradation; cellulosome; protein-protein interaction; calcium;
D O I
10.1073/pnas.0507109103
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Bacterial cell-surface attachment of macromolecular complexes maintains the microorganism in close proximity to extracellular substrates and allows for optimal uptake of hydrolytic byproducts. The cellulosome is a large multienzyme complex used by many anaerobic bacteria for the efficient degradation of plant cell-wall polysaccharides. The mechanism of cellulosome retention to the bacterial cell surface involves a calcium-mediated protein-protein interaction between the dockerin (Doc) module from the cellulosomal scaffold and a cohesin (Coh) module of cell-surface proteins located within the proteoglycan layer. Here, we report the structure of an ultra-high-affinity (K-a = 1.44 x 10(10) M-1) complex between type II Doc, together with its neighboring X module from the cellulosome scaffold of Clostridium thermocellum, and a type II Coh module associated with the bacterial cell surface. Identification of X module-Doc and X module-Coh contacts reveal roles for the X module in Doc stability and enhanced Coh recognition. This extremely tight interaction involves one face of the Coh and both helices of the Doc and comprises significant hydrophobic character and a complementary extensive hydrogen-bond network. This structure represents a unique mechanism for cellsurface attachment in anaerobic bacteria and provides a rationale for discriminating between type I and type II Coh modules.
引用
收藏
页码:305 / 310
页数:6
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