› 3k3k

X-ray diffraction
1.7Å resolution

Crystal structure of dimeric abscisic acid (ABA) receptor pyrabactin resistance 1 (PYR1) with ABA-bound closed-lid and ABA-free open-lid subunits

Released:
DOI: 10.2210/pdb3k3k/pdb
PDB entry 3k3k coloured by chain, front view.
PDB entry 3k3k coloured by chain, side view.
PDB entry 3k3k coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.
Nishimura N, Hitomi K, Arvai AS, Rambo RP, Hitomi C, Cutler SR, Schroeder JI, Getzoff ED
Science 326 1373-9 (2009)
PMID: 19933100

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-129276 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Abscisic acid receptor PYR1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 23.77 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: O49686 (Residues: 1-191; Coverage: 100%)
Gene names: ABIP6, At4g17870, PYR1, RCAR11, T6K21.50
Sequence domains: Polyketide cyclase / dehydrase and lipid transport
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4

Ligands and Environments

1 bound ligand:
Ligand A8S 1 x A8S
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: P2
Unit cell:
a: 50.208Å b: 61.407Å c: 82.844Å
α: 90° β: 98.97° γ: 90°
R-values:
R R work R free
0.191 0.189 0.237
Expression system: Escherichia coli

Quick links

Citations

65 review citations

Abscisic acid: emergence of a core signaling network.
Cutler et al. (2010)
64 more

15 mentions without citation

Evolution of abscisic acid synthesis and signaling mechanisms.
Hauser et al. (2011)
14 more