Figure 2.
Figure 2. Domain delineation of PurS. (A) Structural
representative of the ferredoxin-like fold: the
anticodon-binding domain of PheRS (PDB code: 1pys, chain B). (B)
Dimeric unit of PurS colored according to chains (chain A: blue,
chain B: red). The PurS domain-swapped dimer structure contains
two domains (separated by a black horizontal bar), each of which
resembles the ferredoxin-like fold. The ferredoxin-like fold is
made of four -strands
and two -helices,
and in PurS these structural elements are contributed from the
two chains of the dimer by a domain swap of -helix
H1 and -strand
2.
The elements are labeled according to the ferredoxin-like fold.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2006,
65,
249-254)
copyright 2006.
-strands
and two 
-helices,
and in PurS these structural elements are contributed from the
two chains of the dimer by a domain swap of