› 1u1y

X-ray diffraction
2.85Å resolution

Crystal structure of a complex between WT bacteriophage MS2 coat protein and an F5 aptamer RNA stemloop with 2aminopurine substituted at the-10 position

Released:
DOI: 10.2210/pdb1u1y/pdb
PDB entry 1u1y coloured by chain, front view.
PDB entry 1u1y coloured by chain, side view.
PDB entry 1u1y coloured by chain, top view.
Source organism: Escherichia phage MS2
Primary publication:
The crystal structure of a high affinity RNA stem-loop complexed with the bacteriophage MS2 capsid: further challenges in the modeling of ligand-RNA interactions.
Horn WT, Convery MA, Stonehouse NJ, Adams CJ, Liljas L, Phillips SE, Stockley PG
RNA 10 1776-82 (2004)
PMID: 15496523

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-137138 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 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
5'-R(*CP*CP*GP*GP*(2PR)P*GP*GP*AP*UP*CP*AP*CP*CP*AP*CP*GP*G)-3' Chains: R, S
Molecule details ›
Chains: R, S
Length: 17 nucleotides
Theoretical weight: 5.46 KDa
Source organism: Escherichia phage MS2
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand 2PR 2 x 2PR

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: R32
Unit cell:
a: 288.61Å b: 288.61Å c: 654.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.196
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

11 review citations

SELEX--a (r)evolutionary method to generate high-affinity nucleic acid ligands.
Stoltenburg et al. (2007)
10 more

9 mentions without citation

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