› 7l59

X-ray diffraction
2.68Å resolution

Crystal structure of the dark-adapted full-length bacteriophytochrome XccBphP-G454E variant from Xanthomonas campestris in the Pfr state

Released:
DOI: 10.2210/pdb7l59/pdb
PDB entry 7l59 coloured by chain, front view.
PDB entry 7l59 coloured by chain, side view.
PDB entry 7l59 coloured by chain, top view.
Source organism: Xanthomonas campestris pv. campestris str. 8004
Primary publication:
Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level.
Otero LH, Foscaldi S, Antelo GT, Rosano GL, Sirigu S, Klinke S, Defelipe LA, Sánchez-Lamas M, Battocchio G, Conforte V, Vojnov AA, Chavas LMG, Goldbaum FA, Mroginski MA, Rinaldi J, Bonomi HR
Sci Adv 7 eabh1097 (2021)
PMID: 34818032

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101643 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacteriophytochrome Chain: A
Molecule details ›
Chain: A
Length: 640 amino acids
Theoretical weight: 71.34 KDa
Source organism: Xanthomonas campestris pv. campestris str. 8004
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2XCS3 (Residues: 2-634; Coverage: 100%)
Gene names: XC_4241, bphP
Sequence domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: I41
Unit cell:
a: 182.035Å b: 182.035Å c: 40.059Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.236
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Protein control of photochemistry and transient intermediates in phytochromes.
Salvadori et al. (2022)
4 more

1 mention without citation

Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level.
Otero et al. (2021)