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Figure 3.
Fig. 3. Overall structure of Sto12a. (a) Stereoview of the
Sto12a dimer. α-Helices and β-strands are presented in red and
blue, respectively. The side chains of Cys15, Cys16, and Cys100
are depicted by stick models, and residues and disulfide bridges
are presented in green. The side chains of Asp11 and Lys18 are
shown by stick models, and the residues are presented in yellow,
with the side-chain O atom of Asp11 and the side-chain N atom of
Lys18 presented in red and blue, respectively. The H0–H4
helices and the S1–S3 strands on chain A are indicated. (b) An
end view of the dimer, viewed down the H4 helical axis of chain
A from the N terminus. The colors of chain A are the same as in
(a). Chain B is presented in gray. The H4 helices of chains A
and B are indicated as H4 and H4′, respectively. Residues
Glu72–Arg78 of chain A, and residues Met2–Glu4 and
Glu72–Arg78 of chain B are disordered and are missing from the
figure. The first and last residues in the gap are indicated.
These figures were prepared with PyMol [http://www.pymol.org].
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