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Figure 4.
Figure 4. Structural Analysis of the mDia1 Core FH2
Domain(A) Ribbon diagram of the core FH2 domain. The
NH[2]-terminal, three-helix-bundle, and FH2 motif subdomains are
colored red, blue, and green, respectively. The region
corresponding to the highly conserved ^967GNXMN^971 motif is
colored purple. The NH[2] and COOH termini of the molecule are
indicated by N and C, respectively. Secondary structures are
numbered consecutively. Ile845, Met970, Lys989, Lys994, Lys999,
Arg919, and Asp1067 are shown as ball-and-stick
representation. Distance between Ile845 and Met970 and
approximate locations of the FH1 domain, linker, and DAD in
mDia1 are indicated.(B) A buried salt bridge. A salt bridge
between Arg919 and Asp1067 is shown as ball-and-stick
representation together with surrounding hydrophobic residues,
as indicated.(C) Superimposition of the four molecules in the
asymmetric unit. Molecules A, B, C, and D, colored in red,
green, blue, and yellow, respectively, were superimposed on the
three-helix-bundle subdomains, and are oriented as in (A). Note
that the FH2 subdomain exhibited the highest conformational
differences.(D) Conserved residues. Surface representation of
the mDia1-FH2 core domain with residues conserved in the six
formin family proteins colored orange and those conserved in
five of six colored yellow. Residues mentioned in the text are
indicated. Left and right: orientation as in Figure 3B and
rotated 180°, respectively.
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