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Figure 3.
Figure 3. Dimerization in the TonEBP -DNA complex. a, The
C-terminal dimer interface viewed in the same orientation as
Fig. 1a. Hydrophobic residues Leu 372, Ile 390, Leu 422, Ile
429, and Phe 388 from each TonEBP monomer form the center of the
interface. Polar residues Asn 426, His 424, His 427, Lys 373,
Glu 386, and Ser 375 from each monomer form the peripheral of
the interface through networks of hydrogen bonding and
electrostatic interactions. b, The N-terminal dimer interface
viewed from underneath the DNA with respect to Fig. 1a. The  -helix
of the E'F loop from each monomer supplies residues for
dimerization, which include Arg 315, Ala 317, Asp 318, and Glu
320. The conformation of the -helix
is stabilized by the DNA backbone (N-terminal capping) and by
the hydrophobic interactions with the main body of the protein
through residues Val 321, Leu 312, and Phe 267. c,
Simulated-annealing omit map showing the electron density of the
E'F dimer interface residues (Arg 315, Asn 316, Ala 317, Asp
318, Val 319, and Glu 320) in stereo. The 2.86 Å  [A]-weighted
F[o] - F[c] map is contoured at 2.0 level.
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