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Figure 7.
Figure 7. Comparison of binding surface for enzyme I and
enzyme IIA^Glc on E. coliHPr to the corresponding surface ofB.
subtilis HPr and Crh. The PDB entries used forE. coliHPr, B.
subtilis HPr and Crh are 1HDN,[31] 2HID [40] and 1K1C,
respectively. (a) The residues of helices A and B, involved in
analogous hydrophobic and/or electrostatic interactions in the
(HPr-EIN)E. coli and (HPr-enzyme IIA^Glc)E. coli complexes and
conserved inB. subtilis HPr are highlighted on the HPr surfaces.
The residues, whose side-chains participate in hydrophobic and
electrostatic interactions, are colored in green and blue,
respectively. The PTS active site residue His15 is indicated in
red and the CCR regulation site residue Ser46 in B. subtilis is
indicated in yellow. The corresponding residues of B. subtilis
Crh are colored in the same way but Gln15 of Crh is colored in
magenta. Leu50 of Crh, which is part of the central hydrophobic
core, is colored in dark green. (b) Stick representation of the
residues colored in (a). (c) Same picture as in (a) but
containing also residues situated around the hydrophobic core
involved in hydrophobic and/or electrostatic interactions in the
(HPr-EIN)E. coli and (HPr-enzyme IIA^Glc)E. coli complexes, but
which are only partly conserved in B. subtilis HPr and Crh.
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