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

Oren Yaniv, Ely Morag, Ilya Borovok, Edward A. Bayer, Raphael Lamed, Felix Frolow, Linda J.W. Shimon

Research output: Contribution to journalArticlepeer-review

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 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.

Original languageEnglish
Pages (from-to)733-737
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number7
DOIs
StatePublished - Jul 2013

Keywords

  • CipA
  • Clostridium thermocellum
  • cellulosome
  • family 3 cellulose-binding module

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