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Figure 4.
Structural alignment of Cog4-(525–785) to known COG,
exocyst and Dsl1p subunits. (A) Shown are S. cerevisiae Tip20p
(PDB ID 3FHN, residues 4–701 out of 701) (20), Cog2p (2JQQ,
residues 109–262 out of 262) (14), Sec6p (2FJI, residues
411–805 out of 805) (18), Drosophila melanogaster Sec15 (2A2F,
residues 382–699 out of 766) (19), S. cerevisiae Exo84p (2D2S,
residues 525–753 out of 753) (15), and S. cerevisiae Exo70p
(2PFV, residues 67–623 out of 623) (15–17). Pairwise
alignment was performed with the program DaliLite (47) to match
each of the other structures to Cog4-(525–785). The DaliLite Z
scores for the alignments shown were 12.3 (Cog4-Tip20p), 3.8
(Cog4-Cog2p), 13.1 (Cog4-Sec6p), 10.1 (Cog4-Sec15), 6.2
(Cog4-Exo84p), and 8.0 (Cog4-Exo70p). (B) Cog4- (525–785)
superimposed on proteins containing similar domains C, D, and E.
(C) Stereoview of E domains, aligned using DaliLite and with the
N terminus of each domain indicated by a red sphere. Included,
in addition to the structures cited above, are the E domains of
the cargo-binding domain of S. cerevisiae Myo2p (2F6H) (33) and
the Dsl1p complex subunit Dsl1p (Y. Ren, P.D.J., and F.M.H.,
personal communication). No significant alignment was
discernable for domain E of Tip20p.
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