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6KNA

Viral Ubiquitin from Autographa californica Nucleo Polyhedrosis Virus

Summary for 6KNA
Entry DOI10.2210/pdb6kna/pdb
DescriptorViral ubiquitin (1 entity in total)
Functional Keywordsstructure from cyana 2.1, viral protein
Biological sourceAutographa californica multiple nucleopolyhedrovirus
Total number of polymer chains1
Total formula weight8501.80
Authors
Negi, H.,Reddy, P.P.,Das, R. (deposition date: 2019-08-05, release date: 2020-06-17, Last modification date: 2024-05-15)
Primary citationNegi, H.,Reddy, P.P.,Vengayil, V.,Patole, C.,Laxman, S.,Das, R.
A novel polyubiquitin chain linkage formed by viral Ubiquitin is resistant to host deubiquitinating enzymes.
Biochem.J., 477:2193-2219, 2020
Cited by
PubMed Abstract: The Baculoviridae family of viruses encode a viral Ubiquitin (vUb) gene. Though the vUb is homologous to the host eukaryotic Ubiquitin (Ub), its preservation in the viral genome indicates unique functions that are not compensated by the host Ub. We report the structural, biophysical, and biochemical properties of the vUb from Autographa californica multiple nucleo-polyhedrosis virus (AcMNPV). The packing of central helix α1 to the beta-sheet β1-β5 is different between vUb and Ub. Consequently, its stability is lower compared with Ub. However, the surface properties, ubiquitination activity, and the interaction with Ubiquitin-binding domains are similar between vUb and Ub. Interestingly, vUb forms atypical polyubiquitin chain linked by lysine at the 54th position (K54), and the deubiquitinating enzymes are ineffective against the K54-linked polyubiquitin chains. We propose that the modification of host/viral proteins with the K54-linked chains is an effective way selected by the virus to protect the vUb signal from host DeUbiquitinases.
PubMed: 32478812
DOI: 10.1042/BCJ20200289
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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