Chemistry Reference
In-Depth Information
Fig. 1 (a) Overlaid view of structures of human MT3 (PDB: 2f5h) in
orange
and mouse MT3
(PDB: 1JI9) in
pale green
with the cadmium ions shown as spheres (
left
), and the four metal-
thiolate cluster of human MT3 in the
-domain with the metal ions and sulfur atoms from cysteines
shown in
cyan
and
yellow
respectively (
right
). (b) NMR structures of the
Notothenia coriiceps
Cd
7
MT-nc with the
a
-domain (PDB: 1m0j) (
right
). The
metal-thiolate clusters are also shown with the cadmium ions shown as spheres in
sky blue
and
sulfurs as sticks in
yellow
.(c) Solution structure of bacterial SmtA (PDB: 1jjd) with the zinc ions
shown in pale cyan as spheres (
left
) and the metal cluster Zn
4
Cys
9
His
2
(
right
) with the zinc ions
shown in
pale cyan
, sulfurs in
yellow
, and the nitrogens of histidines in
blue
a
-domain (PDB: 1m0g) (
left
) and the
b
conformations of domains, which renders a proper function of the protein [
50
].
Zinc finger proteins are the most abundant class of zinc-binding proteins that
contain conserved cysteines and histidines coordinated to zinc. Intensive structural
and functional studies have established the invariance of the
framework of the
Cys
2
His
2
zinc finger module and provided a sound basis for understanding the
nature of DNA recognition [
40
,
51
-
55
]. Diverse structures of zinc fingers also
account for their diverse functions such as DNA recognition, RNA packaging,
bba
