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PDBsum entry 5n2e
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References listed in PDB file
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Key reference
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Title
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The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.
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Authors
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N.Tarbouriech,
C.Ducournau,
S.Hutin,
P.J.Mas,
P.Man,
E.Forest,
D.J.Hart,
C.N.Peyrefitte,
W.P.Burmeister,
F.Iseni.
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Ref.
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Nat Commun, 2017,
8,
1455.
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PubMed id
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Abstract
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Vaccinia virus (VACV), the prototype member of the Poxviridae, replicates in the
cytoplasm of an infected cell. The catalytic subunit of the DNA polymerase E9
binds the heterodimeric processivity factor A20/D4 to form the functional
polymerase holoenzyme. Here we present the crystal structure of full-length E9
at 2.7 Å resolution that permits identification of important
poxvirus-specific structural insertions. One insertion in the palm domain
interacts with C-terminal residues of A20 and thus serves as the processivity
factor-binding site. This is in strong contrast to all other family B
polymerases that bind their co-factors at the C terminus of the thumb domain.
The VACV E9 structure also permits rationalization of polymerase inhibitor
resistance mutations when compared with the closely related eukaryotic
polymerase delta-DNA complex.
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