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Figure 1.
Figure 1 Overall architecture of E. coli L/F-transferase. (A)
Stereo view of the E. coli L/F-transferase structure. The
NH[2]-terminal domain (residues 2–62) and the COOH-terminal
domain (residues 63–232) are colored blue and green,
respectively. The puromycin bound to the hydrophobic pocket is
colored yellow. (B) Topology diagram of L/F-transferase. The
rimmed elements in the COOH-terminal domain (  3–
5)
and (  5–
12)
are common to the GNAT superfamily fold. The -helices
and -strands
in the COOH-terminal domains are colored red and yellow,
respectively. (C) Comparison of the structures of E. coli
L/F-transferase (left), W. viridescens FemX (wvFemX; middle, PDB
accession number 1P4N; Biarrotte-Sorin et al, 2004) and S.
aureus FemA (saFemA; PDB accession number 1LRZ; Benson et al,
2002). The COOH-terminal domain of L/F-transferase is
topologically similar to the domain 2's of wvFemX and saFemA.
The conserved -helices
and -strands
in L/F-transferase, wvFemX and saFemA, are colored red and
yellow, respectively.
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