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PDBsum entry 2ztt
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References listed in PDB file
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Key reference
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Title
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Structural insight into the essential pb1-Pb2 subunit contact of the influenza virus RNA polymerase.
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Authors
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K.Sugiyama,
E.Obayashi,
A.Kawaguchi,
Y.Suzuki,
J.R.Tame,
K.Nagata,
S.Y.Park.
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Ref.
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EMBO J, 2009,
28,
1803-1811.
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PubMed id
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Abstract
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Influenza virus RNA-dependent RNA polymerase is a multi-functional heterotrimer,
which uses a 'cap-snatching' mechanism to produce viral mRNA. Host cell mRNA is
cleaved to yield a cap-bearing oligonucleotide, which can be extended using
viral genomic RNA as a template. The cap-binding and endonuclease activities are
only activated once viral genomic RNA is bound. This requires signalling from
the RNA-binding PB1 subunit to the cap-binding PB2 subunit, and the interface
between these two subunits is essential for the polymerase activity. We have
defined this interaction surface by protein crystallography and tested the
effects of mutating contact residues on the function of the holo-enzyme. This
novel interface is surprisingly small, yet, it has a crucial function in
regulating the 250 kDa polymerase complex and is completely conserved among
avian and human influenza viruses.
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