Figure 1.
FIGURE 1. Structure of 2-m and location of
mutations introduced. A, amino acid sequence. Trp^60 and Trp^95
are indicated in red and orange, respectively. Residues mutated
to Trp are Leu^39 (green), Ser^33 (cyan), Val^49 (blue), and
Tyr^78 (purple). A Met is always present at the N terminus of
all the 2-ms, which is indicated
as M0. B, schematic structure. Side chains of Trp^60 and Trp^95
and the residues mutated to Trp are indicated with the same
colors as in A. Secondary structures are indicated by hydrogen
bonds (A) and the numbering of -strands (A and B). The
schematic structure was produced using MOLMOL (43) with our
structure (PDB code 2D4F).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
31061-31069)
copyright 2006.
2-m and location of
mutations introduced. A, amino acid sequence. Trp^60 and Trp^95
are indicated in red and orange, respectively. Residues mutated
to Trp are Leu^39 (green), Ser^33 (cyan), Val^49 (blue), and
Tyr^78 (purple). A Met is always present at the N terminus of
all the