Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 69, Part 7 (July 2013)


structural communications



Acta Cryst. (2013). F69, 733-737    [ doi:10.1107/S174430911301614X ]

Structure of a family 3a carbohydrate-binding module from the cellulosomal scaffoldin CipA of Clostridium thermocellum with flanking linkers: implications for cellulosome structure

O. Yaniv, E. Morag, I. Borovok, E. A. Bayer, R. Lamed, F. Frolow and L. J. W. Shimon

Abstract: 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 Å. The structure is a [beta]-sandwich with a structural Ca2+ 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.

PDB reference: 4jo5

Keywords: family 3 cellulose-binding module; CipA; Clostridium thermocellum; cellulosome.


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