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PDBsum entry 3qb8
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References listed in PDB file
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Key reference
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Title
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Paramecium bursaria chlorella virus 1 encodes a polyamine acetyltransferase.
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Authors
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Z.Charlop-Powers,
J.Jakoncic,
J.R.Gurnon,
J.L.Van etten,
M.M.Zhou.
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Ref.
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J Biol Chem, 2012,
287,
9547-9551.
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PubMed id
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Abstract
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Paramecium bursaria chlorella virus 1 (PBCV-1), a large DNA virus that infects
green algae, encodes a histone H3 lysine 27-specific methyltransferase that
functions in global transcriptional silencing of the host. PBCV-1 has another
gene a654l that encodes a protein with sequence similarity to the GCN5 family
histone acetyltransferases. In this study, we report a 1.5 Å crystal structure
of PBCV-1 A654L in a complex with coenzyme A. The structure reveals a unique
feature of A654L that precludes its acetylation of histone peptide substrates.
We demonstrate that A654L, hence named viral polyamine acetyltransferase (vPAT),
acetylates polyamines such as putrescine, spermidine, cadaverine, and
homospermidine present in both PBCV-1 and its host through a reaction dependent
upon a conserved glutamate 27. Our study suggests that as the first virally
encoded polyamine acetyltransferase, vPAT plays a possible key role in the
regulation of polyamine catabolism in the host during viral replication.
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