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PDBsum entry 3zue
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PDB id:
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Virus
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Title:
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Rabbit hemorrhagic disease virus (rhdv)capsid protein
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Structure:
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Capsid structural protein vp60. Chain: a, b, c. Synonym: vp1. Engineered: yes
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Source:
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Rabbit hemorrhagic disease virus. Organism_taxid: 11976. Strain: ast89. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: h5.
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Authors:
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D.Luque,J.M.Gonzalez,J.Gomez-Blanco,R.Marabini,J.Chichon,I.Mena, I.Angulo,J.L.Carrascosa,N.Verdaguer,B.L.Trus,J.Barcena,J.R.Caston
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Key ref:
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D.Luque
et al.
(2012).
Epitope insertion at the N-terminal molecular switch of the rabbit hemorrhagic disease virus T = 3 capsid protein leads to larger T = 4 capsids.
J Virol,
86,
6470-6480.
PubMed id:
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Date:
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18-Jul-11
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Release date:
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23-May-12
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Headers
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References
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Q86119
(POLG_RHDVA) -
Genome polyprotein from Rabbit hemorrhagic disease virus (strain AST89)
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Seq:
Struc:
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2344 a.a.
547 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 8 residue positions (black
crosses)
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Enzyme class 1:
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E.C.2.7.7.48
- RNA-directed Rna polymerase.
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Reaction:
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RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
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RNA(n)
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+
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ribonucleoside 5'-triphosphate
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=
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RNA(n+1)
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+
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diphosphate
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Enzyme class 2:
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E.C.3.4.22.66
- calicivirin.
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Enzyme class 3:
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E.C.3.6.1.15
- nucleoside-triphosphate phosphatase.
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Reaction:
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a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
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ribonucleoside 5'-triphosphate
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+
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H2O
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=
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ribonucleoside 5'-diphosphate
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+
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phosphate
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Virol
86:6470-6480
(2012)
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PubMed id:
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Epitope insertion at the N-terminal molecular switch of the rabbit hemorrhagic disease virus T = 3 capsid protein leads to larger T = 4 capsids.
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D.Luque,
J.M.González,
J.Gómez-Blanco,
R.Marabini,
J.Chichón,
I.Mena,
I.Angulo,
J.L.Carrascosa,
N.Verdaguer,
B.L.Trus,
J.Bárcena,
J.R.Castón.
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ABSTRACT
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