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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 7(69), p. 733-737, 2013

DOI: 10.1107/s174430911301614x

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

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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 β-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.