› 4m35

X-ray diffraction
2.05Å resolution

Crystal structure of gated-pore mutant H126/141D of second DNA-Binding protein under starvation from Mycobacterium smegmatis

Released:
DOI: 10.2210/pdb4m35/pdb
PDB entry 4m35 coloured by chain, front view.
PDB entry 4m35 coloured by chain, side view.
PDB entry 4m35 coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis.
Williams SM, Chandran AV, Vijayabaskar MS, Roy S, Balaram H, Vishveshwara S, Vijayan M, Chatterji D
J Biol Chem 289 11042-11058 (2014)
PMID: 24573673

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106366 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferritin/DPS protein domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 168 amino acids
Theoretical weight: 18.47 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli
UniProt:
  • Canonical: A0QXB7 (Residues: 1-161; Coverage: 100%)
Gene name: MSMEG_3242
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

3 bound ligands:
Ligand FE2 4 x FE2
Ligand MG 2 x MG
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: R32
Unit cell:
a: 90.23Å b: 90.23Å c: 420.312Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.175 0.206
Expression system: Escherichia coli

Quick links

Citations

3 review citations

An Overview of Dps: Dual Acting Nanovehicles in Prokaryotes with DNA Binding and Ferroxidation Properties.
Williams et al. (2021)
2 more

1 mention without citation

A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis.
Williams et al. (2014)