› 3mw6

X-ray diffraction
2.21Å resolution

Crystal structure of NMB1681 from Neisseria meningitidis MC58, a FinO-like RNA chaperone

Released:
DOI: 10.2210/pdb3mw6/pdb
PDB entry 3mw6 coloured by chain, front view.
PDB entry 3mw6 coloured by chain, side view.
PDB entry 3mw6 coloured by chain, top view.
Source organism: Neisseria meningitidis MC58
Primary publication:
N. meningitidis 1681 is a member of the FinO family of RNA chaperones.
Chaulk S, Lu J, Tan K, Arthur DC, Edwards RA, Frost LS, Joachimiak A, Glover JN
RNA Biol 7 812-9 (2010)
PMID: 21045552

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-191690 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ProQ/FinO domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 144 amino acids
Theoretical weight: 15.93 KDa
Source organism: Neisseria meningitidis MC58
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9JY98 (Residues: 1-141; Coverage: 100%)
Gene name: NMB1681
Sequence domains: ProQ/FINO family
Structure domains: ProQ/FinO domain

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
1 modified residue:
Ligand MSE 18 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 126.479Å b: 76.527Å c: 122.715Å
α: 90° β: 116.84° γ: 90°
R-values:
R R work R free
0.193 0.191 0.235
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

RNA-binding proteins involved in post-transcriptional regulation in bacteria.
Van Assche et al. (2015)
3 more

3 mentions without citation

ProQ/FinO-domain proteins: another ubiquitous family of RNA matchmakers?
Olejniczak et al. (2017)
2 more