1ZV9

Crystal structure analysis of a type II cohesin domain from the cellulosome of Acetivibrio cellulolyticus- SeMet derivative

Summary for 1ZV9

• Entry DOI: 10.2210/pdb1zv9/pdb
• Related: 1QZN 1TYJ
• Descriptor: Cellulosomal scaffoldin adaptor protein B, NITRATE ION, 1,2-ETHANEDIOL, ... (7 entities in total)
• Functional Keywords: cohesins ii; cellulosome, cellulosome
• Biological source: Acetivibrio cellulolyticus
• Total number of polymer chains: 1
• Total formula weight: 19267.93

Authors

Noach, I.,Rosenheck, S.,Lamed, R.,Shimon, L.,Bayer, E.,Frolow, F. (deposition date: 2005-06-01, release date: 2006-06-13, Last modification date: 2024-10-30)

Primary citation

Noach, I.,Frolow, F.,Alber, O.,Lamed, R.,Shimon, L.J.,Bayer, E.A.
Intermodular linker flexibility revealed from crystal structures of adjacent cellulosomal cohesins of Acetivibrio cellulolyticus.
J.Mol.Biol., 391:86-97, 2009

PubMed Abstract: Cellulosome complexes comprise an intercalated set of multimodular dockerin-containing enzymatic subunits connected to cohesin-containing nonenzymatic subunits called scaffoldins. The adjoining modules in each cellulosomal subunit are interconnected by a variety of linker segments of different lengths and composition. The exact role of the cellulosomal linkers has yet to be described, although it is assumed that they contribute to the architecture and action of the cellulosome by providing the protein subunits with flexibility and by providing spacers between the enzymatic modules that could enhance interactions with the cellulose substrate. Here we present four crystal structures of Acetivibrio cellulolyticus cellulosomal type II cohesins with linker extensions. Two of the structures represent two different crystal forms (trigonal and orthorhombic) of the same N-terminal cohesin module (CohB1) together with its full (6-residue) native C-terminal linker, derived from scaffoldin B. The other two structures belong to the adjacent (second) cohesin module (CohB2), each of which was crystallized with the same 6-residue linker segment, but now positioned at the N-terminus and with either a truncated (5-residue) or a full-length (45-residue) C-terminal linker, respectively. Comparison between the two CohB1 structures revealed significant differences in the conformation of their equivalent C-terminal linker segment. In one crystal form a helical conformation was observed, as opposed to an extended conformation in the other. The CohB2 structures also displayed diverse conformations in their linker segments. In these structures, different linker conformations were observed in the individual molecules within the asymmetric unit of each structure. This conformational diversity implies that the linkers may adopt alternative conformations in their natural environment, consistent with varying environmental conditions. The findings suggest that linkers can play an important role in the assembly, dynamics and function of the cellulosomal components.

PubMed: 19501595
DOI: 10.1016/j.jmb.2009.06.006

Experimental method

X-RAY DIFFRACTION (1.28 Å)