4jo5 | pdb_00004jo5

CBM3a-L domain with flanking linkers from scaffoldin cipA of cellulosome of Clostridium thermocellum

spinqualitylabelsall models 4jo5, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jo5 is a 1 chain structure with sequence from Acetivibrio thermocellus YS. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.98Å Ligands: 1MZ, CA, CL, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The cellulosome of the cellulolytic bacterium Clostridium thermocellum has a structural multi-modular protein called CipA (cellulosome-integrating protein A) that includes nine enzyme-binding cohesin modules and a family 3 cellulose-binding module (CBM3a). In the CipA protein, the CBM3a module is located between the second and third cohesin modules and is connected to them via proline/threonine-rich linkers. The structure of CBM3a with portions of the C- and N-terminal flanking linker regions, CBM3a-L, has been determined to a resolution of 1.98 A. The structure is a beta-sandwich with a structural Ca(2+) ion. The structure is consistent with the previously determined CipA CBM structure; however, the structured linker regions provide a deeper insight into the overall cellulosome structure and assembly. Structure of a family 3a carbohydrate-binding module from the cellulosomal scaffoldin CipA of Clostridium thermocellum with flanking linkers: implications for cellulosome structure.,Yaniv O, Morag E, Borovok I, Bayer EA, Lamed R, Frolow F, Shimon LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul;69(Pt 7):733-7. doi:, 10.1107/S174430911301614X. Epub 2013 Jun 27. PMID:23832198 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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