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Fig. 7.7
Interaction of two PYLs molecules in PYLs-(
+
)-ABA structure (
cyan
and
green
).
a
PYL1-(
+
)-ABA (pdb ID: 3JRS) and
b
PYL3-(
+
)-ABA (pdb ID: 4DSC). ABA,
ʱ
4 and gate are
shown. Nitrogen:
blue
, oxygen:
red
Fig. 7.8 a
Structural superimposition of the apo-PYL10 with PYL10-(
+
)-ABA and apo- PYL3
reveals a partially close conformation of the gate loop in the ligand-free PYL10. Apo-PYL10
(PDB: 3RT2) is in
violet
, apo-PYL3 (PDB: 3KLX) in
yellow
, PYL10-(
+
)-ABA (PDB: 3R6P)
and ABA in
cyan
.
b
Structural comparison of ABA-bound PYL10 (
cyan
) and PYL3-(
+
)-ABA
(PDB: 4DSB,
gray
). The ABA molecule in PYL10 is shown as
green sticks
. Leu79 and Lys80 are
at the entrance of the ligand-binding pocket, affecting the ABA-independent inhibition of PP2Cs.
Both the corresponding residues in PYL3 are valine
The recent research had examined the effect of all PYLs (except for PYL7,
11, 12, 13) on inhibiting the phosphatase activity of four PP2Cs, including
ABI1, HAB1, HAB2, and PP2CA, in the presence or absence of ABA (Hao et al.
2011
). They found that a subclass of PYLs proteins, such as PYL10, exhibited
constitutive binding and inhibition of PP2Cs even in the absence of any ligands.
While other PYLs relied on ABA to inhibit PP2Cs. By comparing the structures
between apo-PYL10 and apo-PYL3, we know that the gate loop of the apo-
PYL10 is partially in the closed conformation (see Fig.
7.8
a). Thus, ligand-free
PYL10 is able to adopt a compatible conformation for PP2Cs recognition. By
comparing the structure of apo-PYL10 with other dimeric PYLs (see Fig.
7.8
b),
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