The crystal structure of a type I cohesin domain at 1.7 Å resolution - Institut Pasteur Access content directly
Journal Articles Journal of Molecular Biology Year : 1997

The crystal structure of a type I cohesin domain at 1.7 Å resolution


The quaternary organization of the cellulosome, a multi-enzymatic extracellular complex produced by cellulolytic bacteria, depends on specific interactions between dockerin domains, double EF-hand subunits carried by the catalytic components, and cohesin domains, individual receptor subunits linearly arranged within a non-catalytic scaffolding polypeptide. Cohesin-dockerin complexes with distinct specificities are also thought to mediate the attachment of cellulosomes to the cell membrane. We report here the crystal structure of a single cohesin domain from the scaffolding protein of Clostridium thermocellum. The cohesin domain folds into a nine-stranded beta-sandwich with an overall "jelly roll" topology, similar to that observed in bacterial cellulose-binding domains. Surface-exposed patches of conserved residues promote extensive intermolecular contacts in the crystal, and suggest a possible binding target for the EF-hand pair of the cognate dockerin domain. Comparative studies of cohesin domains indicate that, in spite of low sequence similarities and different functional roles, all cohesin domains share a common nine-stranded beta-barrel fold stabilized by a conserved hydrophobic core. The formation of stable cohesin-dockerin complexes requires the presence of Ca2+. However, the structure of the cohesin domain reported here reveals no obvious Ca2+-binding site, and previous experiments have failed to detect high affinity binding of Ca2+ to the unliganded dockerin domain of endoglucanase CelD. Based on structural and biochemical evidence, we propose a model of the cohesin-dockerin complex in which the dockerin domain requires complexation with its cohesin partner for protein stability and high-affinity Ca2+ binding.

Dates and versions

pasteur-03136642 , version 1 (09-02-2021)



Gisele A. Tavares, Pierre Béguin, Pedro M. Alzari. The crystal structure of a type I cohesin domain at 1.7 Å resolution. Journal of Molecular Biology, 1997, 2002-05-25, 273 (3), pp.701-713. ⟨10.1006/jmbi.1997.1326⟩. ⟨pasteur-03136642⟩


8 View
0 Download



Gmail Facebook X LinkedIn More