|
Figure 1.
Figure 1. The X-ray crystal structure of Sir4p residues
1272-1347. (a) Two C-terminal Sir4 fragments combine to form a
72 residue homodimeric parallel coiled coil, including amino
acid residues V1274 to L1344 (strand A, cyan) or M1345 (strand
S, magenta). Residues in positions a and d are drawn in stick
model. (b) A helical wheel diagram with a and d residues listed.
b-Branching residues are shown in bold, colored are charged or
polar residues (d positions K1288, N1309, T1323, and K1337). (c)
Residues in the coiled coil. Mutations to disrupt the coiled
coil are in bold, and underlined when combined. Interface II
mutants are red.
|
