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Figure 5.
FIG. 5. Structural analysis of amino acid substituted MobA
proteins. Composite figure showing the locations of the
substituted residues in MobA and their effects on the local
structure. The central picture shows a C  trace of the wild type
structure in white (Protein Data Bank accession code 1E5K [PDB]
), with the side chains (or C s for glycines) of the
substituted residues shown in black. The four circular insets
show the local changes in the structures for four of the five
variants whose structures were determined: close-ups of the wild
type (white) and variant (black) structures are superposed. The
R19A variant is not shown, since the resultant model was
virtually indistinguishable from the wild type. In fact, the
side chain of Arg 19 was not visible in the electron density
maps for any of the crystal structures of MobA (including wild
type), although it is included in the central picture for
completeness. Note the change in the conformation of the
consensus loop in the G22L variant and the loss of a salt bridge
in the D101N form of the protein. The perturbations in the N180D
and N182D structures are relatively minor. The figure was
generated using SwissPDBviewer (40) (www.expasy.ch/spdbv) and
rendered using POV-RayTM (www.povray.org).
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