› 1w92

X-ray diffraction
1.7Å resolution

The structure of carbomonoxy murine neuroglobin reveals a heme- sliding mechanism for affinity regulation

Released:
DOI: 10.2210/pdb1w92/pdb
PDB entry 1w92 coloured by chain, front view.
PDB entry 1w92 coloured by chain, side view.
PDB entry 1w92 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity.
Vallone B, Nienhaus K, Matthes A, Brunori M, Nienhaus GU
Proc Natl Acad Sci U S A 101 17351-6 (2004)
PMID: 15548613

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190172 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuroglobin Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 17.02 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ER97 (Residues: 1-151; Coverage: 100%)
Gene name: Ngb
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand HEM 1 x HEM
Ligand CMO 1 x CMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: R32
Unit cell:
a: 88.373Å b: 88.373Å c: 110.983Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.26 0.26 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

22 review citations

Carbon monoxide, reactive oxygen signaling, and oxidative stress.
Piantadosi CA. (2008)
21 more

11 mentions without citation

The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity.
Vallone et al. (2004)
10 more