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X-ray diffraction
2.2Å resolution

Crystal structure of the chromophore-binding domain of an unusual bacteriophytochrome RpBphP3 from R. palustris

Released:
DOI: 10.2210/pdb2ool/pdb
PDB entry 2ool coloured by chain, front view.
PDB entry 2ool coloured by chain, side view.
PDB entry 2ool coloured by chain, top view.
Source organism: Rhodopseudomonas palustris CGA009
Primary publication:
Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion.
Yang X, Stojkovic EA, Kuk J, Moffat K
Proc Natl Acad Sci U S A 104 12571-6 (2007)
PMID: 17640891

Function and Biology Details

Reaction catalysed: 
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
histidine kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37.33 KDa
Source organism: Rhodopseudomonas palustris CGA009
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6N5G2 (Residues: 1-337; Coverage: 44%)
Gene names: RPA3016, TX73_015620, phyB2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand LBV 2 x LBV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C, APS BEAMLINE 19-ID
Spacegroup: P321
Unit cell:
a: 151.866Å b: 151.866Å c: 75.996Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.188 0.231
Expression system: Escherichia coli BL21(DE3)

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Citations

23 review citations

Structure and function of plant photoreceptors.
Möglich et al. (2010)
22 more

15 mentions without citation

Structure and signaling mechanism of Per-ARNT-Sim domains.
Möglich et al. (2009)
14 more