6suq

X-ray diffraction
3.7Å resolution

Crystal Structure of TcdB2-TccC3-TEV

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear inclusion protein A; TccC3; TcdB2 Chain: A
Molecule details ›
Chain: A
Length: 2410 amino acids
Theoretical weight: 272.97 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P04517 (Residues: 2038-2273; Coverage: 8%)
  • Canonical: Q8GF97 (Residues: 1-680; Coverage: 71%)
  • Canonical: Q8GF99 (Residues: 1-1474; Coverage: 100%)
Gene names: TccC3, tcdB2
Sequence domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3221
Unit cell:
a: 234.43Å b: 234.43Å c: 143.19Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.269 0.269 0.302
Expression system: Escherichia coli