Open AccessStructure of a family 3a carbohydrate‐binding module from the cellulosomal scaffoldin CipA of Clostridium thermocellum with flanking linkers: implications for cellulosome structure
Author(s) -
Yaniv Oren,
Morag Ely,
Borovok Ilya,
Bayer Edward A.,
Lamed Raphael,
Frolow Felix,
Shimon Linda J. W.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911301614x
Subject(s) - clostridium thermocellum , cellulosome , linker , cohesin , chemistry , carbohydrate binding module , biochemistry , glycoside hydrolase , cellulase , biophysics , cellulose , chromatin , biology , enzyme , dna , computer science , operating system
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.