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Figure 1.
Crystal structure and the simulated-annealing F [o] --F [c]
omit map in the conserved region of AscE. (A) The map is
contoured at a level of 2.0 [sigma]. Residues Leu24 to Ala27 and
all atoms within 3.0 A of Leu24 to Ala27 were omitted prior to
refinement. (B) Ribbon representation of the crystal structure
of the dimeric AscE from residue Pro14 to Glu65 at two different
angles. The hydrophobic residues (Leu20, Leu24, Ala27, Val31,
Trp47, Ala53, Ile60, and Ile64) that form an interlocking
network at the dimeric interface of the protein are shown in a
ball-and-stick model. The figure was generated with the program
Chimera (Pettersen et al. 2004). (C) Overlay of the crystal
structures of AscE (purple) and YscE (chain A and B) (cyan)
viewed at two different angles. The dimers of AscE and YscE
overlay with an RMSD of 2.2 A for 101 C[[alpha]] atoms using
DaliLite pairwise comparison of protein structure. (D) Ribbon
representation of the structures of PscE (green) and YscE
(yellow) as in the crystal structures of the complexes
PscE-PscF^55 --85-PscG and YscEFG viewed at two different angles
(Quinaud et al. 2007; Sun et al. 2008). Figure 1A Figure 1.- was
prepared using the program PyMOL (DeLano Scientific). Figure 1B
--D Figure 1.-was
prepared using the program Chimera (Pettersen et al. 2004).
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