› 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 1w92 coloured by chain and viewed from the front.
PDB 1w92 coloured by chain and viewed from the side.
PDB 1w92 coloured by chain and viewed from the top.
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)
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

Structural and (Pseudo-)Enzymatic Properties of Neuroglobin: Its Possible Role in Neuroprotection.
De Simone et al. (2021)
21 more

10 mentions without citation

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