› 6zh5

Electron Microscopy
2.7Å resolution

Folding of an iron binding peptide in response to sedimentation is resolved using ferritin as a nano-reactor

Released:
DOI: 10.2210/pdb6zh5/pdb
PDB entry 6zh5 coloured by chain, front view.
PDB entry 6zh5 coloured by chain, side view.
PDB entry 6zh5 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Folding of an Intrinsically Disordered Iron-Binding Peptide in Response to Sedimentation Revealed by Cryo-EM.
Davidov G, Abelya G, Zalk R, Izbicki B, Shaibi S, Spektor L, Shagidov D, Meyron-Holtz EG, Zarivach R, Frank GA
J Am Chem Soc 142 19551-19557 (2020)
PMID: 33166133
Related structures: EMD-11214

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151447 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferritin light chain 1 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, Z
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, Z
Length: 216 amino acids
Theoretical weight: 24.36 KDa
Source organism: Mus musculus
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P29391 (Residues: 1-183; Coverage: 100%)
Gene names: Ftl, Ftl-1, Ftl1
Sequence domains: Ferritin-like domain

Ligands and Environments

1 bound ligand:
Ligand FE 16 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.7Å
Relevant EMDB volumes: EMD-11214
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

1 citations in other articles

SAMase of Bacteriophage T3 Inactivates Escherichia coli's Methionine S-Adenosyltransferase by Forming Heteropolymers.
Simon-Baram et al. (2021)

1 mention without citation

Folding of an Intrinsically Disordered Iron-Binding Peptide in Response to Sedimentation Revealed by Cryo-EM.
Davidov et al. (2020)