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
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: