2der

X-ray diffraction
3.1Å resolution

Cocrystal structure of an RNA sulfuration enzyme MnmA and tRNA-Glu in the initial tRNA binding state

Released:
Source organism: Escherichia coli
Primary publication:
Snapshots of tRNA sulphuration via an adenylated intermediate.
Nature 442 419-24 (2006)
PMID: 16871210

Function and Biology Details

Reaction catalysed:
A [protein]-S-sulfanyl-L-cysteine + uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate + acceptor
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-150571 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
tRNA-specific 2-thiouridylase MnmA Chains: A, B
Molecule details ›
Chains: A, B
Length: 380 amino acids
Theoretical weight: 42.41 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P25745 (Residues: 1-368; Coverage: 100%)
Gene names: JW1119, asuE, b1133, mnmA, trmU, ycfB
Sequence domains:
Structure domains:
tRNA Chains: C, D
Molecule details ›
Chains: C, D
Length: 76 nucleotides
Theoretical weight: 24.38 KDa
Source organism: Escherichia coli
Expression system: Not provided
Sequence domains: tRNA

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2
Unit cell:
a: 225.389Å b: 175.845Å c: 52.965Å
α: 90° β: 101.62° γ: 90°
R-values:
R R work R free
0.219 0.219 0.269
Expression systems:
  • Escherichia coli
  • Not provided