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Figure 4.
Figure 4 Comparison of human and bacterial GS. (A)
Structure-based sequence alignment of hGS and ecGS. The
secondary structure and residue numbering of hGS are shown above
the alignment and the ecGS numbering below it. The secondary
structure of the conserved structural core elements of the
ATP-grasp superfamily are coloured as follows: the N-terminal
domain is red, the middle, lid domain is green, the C-terminal
domain is blue and the linker region (to the lid domain) in
orange. Additional secondary structures found in hGS are shown
in gray. Strictly conserved residues are highlighted in darkened
boxes and invariant residues of GS enzymes from eukaryotic
organisms are designated by asterisks. The complimentary
mutations and cis-peptide regions discussed in the text are
highlighted in the open boxes. The figure was produced using
ALSCRIPT (Barton, 1993). (B and C) Topological diagrams
highlighting the major structural elements of hGS and ecGS. The
colours refer to the structural cores conserved throughout the
ATP-grasp superfamily. (D and E) Ribbon diagrams of hGS and ecGS
using the same colour coding as in (A). The ribbon figures were
drawn with MOLSCRIPT (Kraulis, 1991).
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