3QB8

Paramecium Chlorella Bursaria Virus1 Putative ORF A654L is a Polyamine Acetyltransferase

Summary for 3QB8

• Entry DOI: 10.2210/pdb3qb8/pdb
• Descriptor: A654L protein, COENZYME A, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: gnat n-acetyltransferase, acetyltransferase, coa, spermine, spermidine, transferase
• Biological source: Paramecium bursaria Chlorella virus 1 (PBCV-1)
• Total number of polymer chains: 2
• Total formula weight: 46516.01

Authors

Charlop-Powers, Z.,Zhou, M.-M.,Jakoncic, J.,Gurnon, J.,Van Etten, J. (deposition date: 2011-01-12, release date: 2012-01-25, Last modification date: 2024-02-21)

Primary citation

Charlop-Powers, Z.,Jakoncic, J.,Gurnon, J.R.,Van Etten, J.L.,Zhou, M.M.
Paramecium bursaria chlorella virus 1 encodes a polyamine acetyltransferase.
J. Biol. Chem., 287:9547-9551, 2012

PubMed Abstract: 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.

PubMed: 22277659
DOI: 10.1074/jbc.C111.337816

Experimental method

X-RAY DIFFRACTION (1.5 Å)