4JO5

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

Summary for 4JO5

• Entry DOI: 10.2210/pdb4jo5/pdb
• Related: 1ANU 1NBC
• Descriptor: Cellulosome anchoring protein cohesin region, CALCIUM ION, GLYCEROL, ... (7 entities in total)
• Functional Keywords: cbm, scaffolding, cellulose binding, beta sandwich, thermophile, cipa module, cellulose binding protein
• Biological source: Clostridium thermocellum
• Total number of polymer chains: 1
• Total formula weight: 21071.09

Authors

Shimon, L.J.W.,Frolow, F.,Bayer, E.A.,Yaniv, O.,Lamed, R.,Morag, E. (deposition date: 2013-03-16, release date: 2013-07-17, Last modification date: 2023-09-20)

Primary citation

Yaniv, O.,Morag, E.,Borovok, I.,Bayer, E.A.,Lamed, R.,Frolow, F.,Shimon, L.J.
Structure of a family 3a carbohydrate-binding module from the cellulosomal scaffoldin CipA of Clostridium thermocellum with flanking linkers: implications for cellulosome structure.
Acta Crystallogr.,Sect.F, 69:733-737, 2013

PubMed 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.

PubMed: 23832198
DOI: 10.1107/S174430911301614X

Experimental method

X-RAY DIFFRACTION (1.98 Å)