› 4u99

X-ray diffraction
2Å resolution

Crystal structure of an H-NOX protein from S. oneidensis in the Fe(II) ligation state, Q154A/Q155A/K156A mutant

Released:
DOI: 10.2210/pdb4u99/pdb
PDB entry 4u99 coloured by chain, front view.
PDB entry 4u99 coloured by chain, side view.
PDB entry 4u99 coloured by chain, top view.
Source organism: Shewanella oneidensis MR-1
Primary publication:
Structural insights into the role of iron-histidine bond cleavage in nitric oxide-induced activation of H-NOX gas sensor proteins.
Herzik MA, Jonnalagadda R, Kuriyan J, Marletta MA
Proc Natl Acad Sci U S A 111 E4156-64 (2014)
PMID: 25253889

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-184371 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme NO-binding domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 187 amino acids
Theoretical weight: 21.16 KDa
Source organism: Shewanella oneidensis MR-1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8EF49 (Residues: 1-181; Coverage: 100%)
Gene name: SO_2144
Sequence domains: Haem-NO-binding
Structure domains: H-NOX domain

Ligands and Environments

3 bound ligands:
Ligand HEM 2 x HEM
Ligand ZN 2 x ZN
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P6322
Unit cell:
a: 164.003Å b: 164.003Å c: 101.718Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.172 0.191
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Nitric oxide, interorganelle communication, and energy flow: a novel route to slow aging.
Valerio et al. (2015)
9 more

9 mentions without citation

Physiological activation and deactivation of soluble guanylate cyclase.
Horst et al. (2018)
8 more