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Figure 6.
Figure 6. Overview of the structure of T. elongatus KaiA(174
-283) (the C-terminal clock-oscillator domain). (a) C  backbone
of a KaiA(174 -283) subunit. h1 (residues 174 -181), red; h2
(186 -203), orange; h3 (211 -225), pink; h4 (229 -247), green;
h5 (255 -258), blue; h6 (260 -277), cyan. (b) A hydrophobic core
formed by Phe177, Phe178, Phe223, Phe224 and Tyr275 connecting
h1, h3 and h6. The helices are colored as described above. The
residues are in ball-and-stick representation (black, carbon;
red, oxygen; yellow, sulfur). (c) A hydrophobic core formed by
Tyr197, Tyr204, Phe205, Phe218, Met240, Phe243, Leu257, Tyr260
and Leu264. (d) C backbone
of a dimer. Yellow, A-chain; purple, B-chain. The eight residues
(Arg179, Asp226, Ile227, Val229, Asp259, Arg261, Glu273 and
Arg276) involved in dimer formation are indicated in
ball-and-stick, as are the functionally essential residue
(His270) and its neighboring residues (Asp266 and Tyr204).
Carbon, black; nitrogen, blue; oxygen, red. Green dotted lines,
hydrogen bonds involved in dimer formation; cyan dotted lines,
hydrogen bonds connecting His270, Asp266 and Tyr204, linearly
arrayed. (e) Space-filling representation of a dimer. The 23
residues conserved in the 11 strains are green, except for
His270, which is red. (f) View of e from a different angle.
Figures of molecular models were prepared with MolScript34 and
Raster3D^35.
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