2zf9

Crystal structure of a type III cohesin module from the cellulosomal ScaE cell-surface anchoring scaffoldin of Ruminococcus flavefaciens

spinqualitylabelsall models 2zf9, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zf9 is a 4 chain structure with sequence from Ruminococcus flavefaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: CL, GOL, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4A3Y2_RUMFL Publication Abstract from PubMed The cellulosome is an intriguing multienzyme complex found in cellulolytic bacteria that plays a key role in the degradation of plant cell-wall polysaccharides. In Ruminococcus flavefaciens, a predominant fiber-degrading bacterium found in ruminants, the cellulosome is anchored to the bacterial cell wall through a relatively short ScaE scaffoldin. Determination of the crystal structure of the lone type-III ScaE cohesin from R. flavefaciens (Rf-CohE) was initiated as a part of a structural effort to define cellulosome assembly. The structure was determined at 1.95 A resolution by single-wavelength anomalous diffraction. This is the first detailed description of a crystal structure for a type-III cohesin, and its features were compared with those of the known type-I and type-II cohesin structures. The Rf-CohE module folds into a nine-stranded beta-sandwich with jellyroll topology, typically observed for cohesins, and includes two beta-flaps in the midst of beta-strands 4 and 8, similar to the type-II cohesin structures. However, the presence in Rf-CohE of an additional 13-residue alpha-helix located between beta-strands 8 and 9 represents a dramatic divergence from other known cohesin structures. The prominent alpha-helix is enveloped by an extensive N-terminal loop, not observed in any other known cohesin, which embraces the helix presumably enhancing its stability. A planar surface at the upper portion of the front face of the molecule, bordered bybeta-flap 8, exhibits plausible dimensions and exposed amino acid residues to accommodate the dockerin-binding site. Proteins 2009. (c) 2009 Wiley-Liss, Inc. Cohesin diversity revealed by the crystal structure of the anchoring cohesin from Ruminococcus flavefaciens.,Alber O, Noach I, Rincon MT, Flint HJ, Shimon LJ, Lamed R, Frolow F, Bayer EA Proteins. 2009 May 18;77(3):699-709. PMID:19544570 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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