    5.1.1.7 | dimer |
CgDapF functions as a dimer and the asymmetric unit contains a CgDapF dimer, the dimerization interface is mainly constituted by the contacts between beta16 from both monomers, and contact between two beta-strands connects the two beta-sheets of the N-terminal domains (NTDs) from both monomers. Contacts between the connecting loops (alpha1-beta3) from both monomers also mediate dimerization of the protein. Each CgDapF monomer consists of two distinct domains: an NTD (Met1-Asp131 and Gly268-Ile277) and a C-terminal domain (CTD, Met132-Thr267). Each domain contains a set of five-stranded and three-stranded antiparallel beta-sheets and two alpha-helices. One alpha-helix of each domain (alpha2 in the NTD and alpha4 in the CTD) is sandwiched between the five-stranded and three-stranded beta-sheets, whereas the other helix lies on the surface of the protein. The NTD and the CTD are structurally homologous to each other, structure comparisons of DAP epimerases, overview |
-, 749346 |
