   2.8.3.21 | crystal structures of apo-CaiB, as well as its Asp169Ala mutant bound to CoA and to carnitinyl-CoA, to 1.6, 2.4, and 2.4 A resolution, respectively. CaiB is composed of two identical circular chains that together form an intertwined dimer. Each monomer consists of a large domain, containing a Rossmann fold, and a small domain. The CoA cofactor-binding site is formed at the interface of the large domain of one monomer and the small domain from the second monomer. Most of the protein-CoA interactions are formed with the Rossmann fold domain. CoA binding results in a change in the relative positions of the large and small domains compared with apo-CaiB |
