|
Figure 4.
The NMR structure of the Andes virus G1 tail zinc-binding
domain reveals two classical ββα fold zinc fingers that are
joined together. A, stereoview of the superposition of 20 lowest
energy NMR structures. B and C, ribbon structures of the lowest
energy NMR structure showing the residues involved in the first
(ZF1) (B) and second (ZF2) (C) zinc fingers. Shown are the
cysteine and histidine residues (yellow) that coordinate Zn^2+
ions (gray) as well as the secondary structures (α[1]-α[2],
β[1]-β[2]). The dual hantaviral G1 zinc fingers interact with
each other and form a single domain with a novel fold as
revealed by DALI (40) and TM-align (41) structural homology
searches.
|
