PDBe 1lvb

X-ray diffraction
2.2Å resolution

CATALYTICALLY INACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH SUBSTRATE

Released:

Function and Biology Details

Reactions catalysed:
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.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero 16-mer
hetero octamer
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nuclear inclusion protein A Chains: A, B
Molecule details ›
Chains: A, B
Length: 243 amino acids
Theoretical weight: 28 KDa
Source organism: Tobacco etch virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04517 (Residues: 2038-2273; Coverage: 8%)
Structure domains: Trypsin-like serine proteases
Capsid protein Chains: C, D
Molecule details ›
Chains: C, D
Length: 10 amino acids
Theoretical weight: 1.16 KDa
Source organism: Tobacco etch virus
Expression system: Not provided
UniProt:
  • Canonical: P04517 (Residues: 2785-2794; Coverage: 0%)

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P42212
Unit cell:
a: 125.317Å b: 125.317Å c: 127.933Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.236 0.263
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided