Cohesin-dockerin interaction in cellulosome assembly. A single hydroxyl group of a dockerin domain distinguishes between nonrecognition and high affinity recognition.

Adva Mechaly, Henri-Pierre Fierobe, Anne Belaich, Jean-Pierre Belaich, Raphael Lamed, Yuval Shoham, and Edward A. Bayer

There was an omission in Table V of the above manuscript. Only 2 of the 9 rows, which contained BIAcore data, were published. The omitted data are crucial for the general message of the article and for the complete understanding of Fig. 2. The complete Table V follows.

                              
View this table:
[in this window]
[in a new window]
 
Table V
Affinity constants for binding of wild-type and mutant dockerin-borne enzymes to immobilized cohesins
The immobilized cohesin receptors and enzyme ligands were derived from C. thermocellum (ct) and C. cellulolyticum (cc). Values were obtained by surface plasmon resonance using a BIAcore system.