Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps
Fig 4
Crystal structures of AquaCyp293 and AquaCyp300.
Domain architecture and topology of AquaCyp293 (A) and AquaCyp300 (B). The cyclophilin fold in grey consists of an eight stranded-antiparallel β-barrel and two α-helices covering the top and the bottom of the barrel. The disulfide bridge (yellow) is shown in stick representation. The additional N-terminal-, insertion, and C-terminal structural elements are coloroured in blue, green and red, respectively.
