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Figure 1.
Figure 1. Structural comparison of the subunit conformations of
PfuCP (open), TthCP (open) and BsuCP (closed). (A) Ribbons
diagram of PfuCP (PDB ID: 1KA2) colored in pink with the  -helices
of the subdomain associated with the groove closure in red. The
residues forming the metal active site are shown in ball and
stick. The bound Mg ion is colored in green and the remaining
ions in CPK. (B) Ribbons diagram of TthCP in the same
orientation colored in tan with the -helices
of the subdomain associated with the conformational change in
green. The residues forming the metal active site are shown in
ball and stick. (C) Ribbons diagram of BsuCP subunit colored in
cyan with the -helices
of the subdomain associated with the conformational change in
blue. The residues forming the zinc active site are shown in
ball and stick. The zinc ion is colored in orange and the
remaining ions in CPK. (D) Overlap of the TthCP (colored in tan
and green) and BsuCP (colored in cyan and blue) structures
aligned based on their common HEXXH motif. The subdomain
exhibiting the largest shift is colored in green and blue,
respectively. (E) Surface diagram of PfuCP showing the open
conformation of the groove. The green color indicates the
location of the metal active site. (F) Surface diagram of TthCP
showing the open conformation of the groove. (G) Surface diagram
of BsuCP showing closed groove conformation.
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