› 6vjv

X-ray diffraction
1.59Å resolution

Crystal structure of the Prochlorococcus phage (myovirus P-SSM2) ferredoxin at 1.6 Angstroms

Released:
DOI: 10.2210/pdb6vjv/pdb
PDB entry 6vjv coloured by chain, front view.
PDB entry 6vjv coloured by chain, side view.
PDB entry 6vjv coloured by chain, top view.
Source organism: Prochlorococcus phage P-SSM2
Primary publication:
Prochlorococcus phage ferredoxin: structural characterization and electron transfer to cyanobacterial sulfite reductases.
Campbell IJ, Olmos JL, Xu W, Kahanda D, Atkinson JT, Sparks ON, Miller MD, Phillips GN, Bennett GN, Silberg JJ
J Biol Chem 295 10610-10623 (2020)
PMID: 32434930

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2Fe-2S ferredoxin-type domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 96 amino acids
Theoretical weight: 10.38 KDa
Source organism: Prochlorococcus phage P-SSM2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q58M74 (Residues: 2-97; Coverage: 99%)
Gene names: PCMG_00283, PSSM2_281
Sequence domains: 2Fe-2S iron-sulfur cluster binding domain

Ligands and Environments

3 bound ligands:
Ligand FES 2 x FES
Ligand ACT 4 x ACT
Ligand ZN 14 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 52.619Å b: 31.446Å c: 61.288Å
α: 90° β: 92.48° γ: 90°
R-values:
R R work R free
0.18 0.178 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

A cellular selection identifies elongated flavodoxins that support electron transfer to sulfite reductase.
Truong et al. (2023)
1 more

1 mention without citation

Prochlorococcus phage ferredoxin: structural characterization and electron transfer to cyanobacterial sulfite reductases.
Campbell et al. (2020)