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PDBsum entry 1tp7
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References listed in PDB file
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Key reference
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Title
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Crystal structure of complete rhinovirus RNA polymerase suggests front loading of protein primer.
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Authors
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T.C.Appleby,
H.Luecke,
J.H.Shim,
J.Z.Wu,
I.W.Cheney,
W.Zhong,
L.Vogeley,
Z.Hong,
N.Yao.
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Ref.
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J Virol, 2005,
79,
277-288.
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PubMed id
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Abstract
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Picornaviruses utilize virally encoded RNA polymerase and a uridylylated protein
primer to ensure replication of the entire viral genome. The molecular details
of this mechanism are not well understood due to the lack of structural
information. We report the crystal structure of human rhinovirus 16 3D
RNA-dependent RNA polymerase (HRV16 3Dpol) at a 2.4-A resolution, representing
the first complete polymerase structure from the Picornaviridae family. HRV16
3Dpol shares the canonical features of other known polymerase structures and
contains an N-terminal region that tethers the fingers and thumb subdomains,
forming a completely encircled active site cavity which is accessible through a
small tunnel on the backside of the molecule. The small thumb subdomain
contributes to the formation of a large cleft on the front face of the
polymerase which also leads to the active site. The cleft appears large enough
to accommodate a template:primer duplex during RNA elongation or a protein
primer during the uridylylation stage of replication initiation. Based on the
structural features of HRV16 3Dpo1 and the catalytic mechanism known for all
polymerases, a front-loading model for uridylylation is proposed.
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