Figure 2
Dimeric structure of TvCyP1 by x-ray crystallography. (a) Structure of TvCyP1 dimer showing secondary structural elements (PDB: 5YB9). The divergent loop of TvCyP1 is highlighted in red. (b) Structural alignment of TvCyP1 protomer (blue) with HcypA (orange). Both structures show the typical cyclophilin fold and exhibit high similarity. (c) Surface representation of TvCyP1 highlighting the active site pocket and S2 pocket. The active site residues and “gatekeeper” residues that guard the S2 pocket are shown in sticks. The structure shows the antiparallel nature of TvCyP1 homodimer. (d and e) Close-up views of polar/salt bridge (d) and hydrophobic interactions (e) at TvCyP1 dimer interface. The residues that form a dimer interface from either of the protomers are shown in different colored sticks. Dotted lines indicate hydrogen bond/salt bridge interactions. Oxygen, nitrogen and sulfur atoms are shown in red, blue and yellow, respectively.
