› 3prp

X-ray diffraction
1.7Å resolution

Structural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic Fever virus in complex with human ubiquitin

Released:
DOI: 10.2210/pdb3prp/pdb
PDB entry 3prp coloured by chain, front view.
PDB entry 3prp coloured by chain, side view.
PDB entry 3prp coloured by chain, top view.
Source organisms:
Primary publication:
Structural analysis of a viral ovarian tumor domain protease from the Crimean-Congo hemorrhagic fever virus in complex with covalently bonded ubiquitin.
Capodagli GC, McKercher MA, Baker EA, Masters EM, Brunzelle JS, Pegan SD
J Virol 85 3621-30 (2011)
PMID: 21228232

Function and Biology Details

Reactions catalysed: 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125312 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RNA-directed RNA polymerase L Chains: A, C
Molecule details ›
Chains: A, C
Length: 178 amino acids
Theoretical weight: 20.39 KDa
Source organism: Orthonairovirus haemorrhagiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6TQR6 (Residues: 1-170; Coverage: 4%)
Gene name: L
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A
Ubiquitin-like domain-containing protein Chains: B, D
Molecule details ›
Chains: B, D
Length: 76 amino acids
Theoretical weight: 8.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: J3QS39 (Residues: 1-75; Coverage: 81%)
Gene name: UBB
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: I222
Unit cell:
a: 79.316Å b: 105.845Å c: 113.032Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.212
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli BL21

Quick links

Citations

13 review citations

Recent advances in the molecular and cellular biology of bunyaviruses.
Walter et al. (2011)
12 more

10 mentions without citation

Strategies of highly pathogenic RNA viruses to block dsRNA detection by RIG-I-like receptors: hide, mask, hit.
Zinzula et al. (2013)
9 more