Figure 1 - full size


Figure 1.
Figure 1 Structure of TcMIP. (A) Amino acid sequence alignment of TcMIP (SWISSPROT entry MIP_TRYCR) with bacterial MIPs from L. pneumophila (SWISSPROT entry MIP_LEGPN), Vibrio cholerae (SWISSPROT entry Q9KP11) and C. trachomatis (SWISSPROT entry MIP_CHLTR), with human FKBP12 (SWISSPROT entry FKB1_HUMAN) and FKBP-like protein from E. coli (SWISSPROT entry FKBB_ECOLI). Residues conserved in all sequences are highlighted in green, those identical to TcMIP in yellow. Signal peptide regions have been omitted. Residues forming the hydrophobic active-site pocket are indicated by blue triangles. The numbering and the secondary structure elements of TcMIP are displayed above the alignment. -Helices are shown in red, -strands in green. (B) Overall structure of TcMIP, with the secondary structure elements shown in red ( -helices) and green ( -strands). The side chains of important residues in the active site of the enzyme are depicted as ball-and-stick models, with carbon atoms in yellow, oxygens in red and nitrogens in blue.

The above figure is reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO Rep (2002, 3, 88-94) copyright 2002.