› 6msf

X-ray diffraction
2.8Å resolution

F6 APTAMER MS2 COAT PROTEIN COMPLEX

Released:
DOI: 10.2210/pdb6msf/pdb
PDB entry 6msf coloured by chain, front view.
PDB entry 6msf coloured by chain, side view.
PDB entry 6msf coloured by chain, top view.
Source organism: Escherichia phage MS2
Primary publication:
Crystal structure of an RNA aptamer-protein complex at 2.8 A resolution.
Convery MA, Rowsell S, Stonehouse NJ, Ellington AD, Hirao I, Murray JB, Peabody DS, Phillips SE, Stockley PG
Nat Struct Biol 5 133-9 (1998)
PMID: 9461079

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero 300-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137162 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct RNA molecules
Macromolecules (3 distinct):
Capsid protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 129 amino acids
Theoretical weight: 13.74 KDa
Source organism: Escherichia phage MS2
Expression system: Escherichia coli
UniProt:
  • Canonical: P03612 (Residues: 2-130; Coverage: 99%)
Sequence domains: Levivirus coat protein
Structure domains: MS2 Viral Coat Protein
RNA (5'-R(*CP*CP*AP*CP*AP*GP*UP*CP*AP*CP*UP*GP*GP*G)-3') Chain: R
Molecule details ›
Chain: R
Length: 14 nucleotides
Theoretical weight: 4.46 KDa
Source organism: Escherichia phage MS2
Expression system: Not provided
RNA (5'-R(*CP*AP*GP*UP*CP*AP*CP*UP*GP*G)-3') Chain: S
Molecule details ›
Chain: S
Length: 10 nucleotides
Theoretical weight: 3.18 KDa
Source organism: Escherichia phage MS2
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: R32
Unit cell:
a: 287.58Å b: 287.58Å c: 652.19Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.201
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

19 review citations

Aptamers come of age - at last.
Bunka et al. (2006)
18 more

5 mentions without citation

Characterization of aptamer-protein complexes by X-ray crystallography and alternative approaches.
Ruigrok et al. (2012)
4 more