4fl4 | pdb_00004fl4

Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome

spinqualitylabelsall models 4fl4, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fl4 is a 12 chain structure with sequence from Atcc 27405. This structure supersedes the now removed PDB entry 3p0d. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, SO4 Gene: Cther_2220 (ATCC 27405), sdbA (ATCC 27405), ClothDRAFT_2952 (ATCC 27405) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Cellulosomes are multi-enzyme complexes responsible for efficient degradation of plant cell wall polysaccharides. The non-enzymatic scaffoldin subunit provides a platform for cellulolytic enzyme binding that enhances the overall activity of the bound enzymes. Understanding the unique quaternary structural elements responsible for the enzymatic synergy of the cellulosome is hindered by the large size and inherent flexibility of these multi-protein complexes. Herein, we have used X-ray crystallography, small angle X-ray scattering (SAXS), and molecular dynamics (MD) to structurally characterize a ternary protein complex from the Clostridium thermocellum cellulosome that comprises a C-terminal trimodular fragment of the CipA scaffoldin bound to the SdbA type-II cohesin module and the type-I dockerin module from the Cel9D glycoside hydrolase. This complex represents the largest fragment of the cellulosome solved by X-ray crystallography to date and reveals two rigid domains, formed by the type-I cohesin:dockerin complex and by the X module-type-II cohesin:dockerin complex, which are separated by a 13-residue linker in an extended conformation. The type-I dockerin modules of the four structural models found in the asymmetric unit are in an alternate orientation to that previously observed, which provides further direct support for the dual mode of binding. Conserved intermolecular contacts between symmetry-related complexes were also observed and may play a role in higher order cellulosome structure. SAXS and MD simulations of the ternary complex revealed that the 13-residue intermodular linker of the scaffoldin subunit is highly dynamic in solution. These studies provide fundamental insights into modular positioning, linker flexibility, and higher order organization of the cellulosome. Scaffoldin conformation and dynamics revealed by a ternary complex from the Clostridium thermocellum cellulosome.,Currie MA, Adams JJ, Faucher F, Bayer EA, Jia Z, Smith SP J Biol Chem. 2012 Jun 15. PMID:22707718 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA