2ga9
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(New page: 200px<br /><applet load="2ga9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ga9, resolution 2.300Å" /> '''Crystal Structure o...)
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Revision as of 08:57, 21 November 2007
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Crystal Structure of the Heterodimeric Vaccinia Virus Polyadenylate Polymerase with Bound ATP-gamma-S
Overview
Polyadenylation of mRNAs in poxviruses, crucial for virion maturation, is, carried out by a poly(A) polymerase heterodimer composed of a catalytic, component, VP55, and a processivity factor, VP39. The ATP-gamma-S bound, and unbound crystal structures of the vaccinia polymerase reveal an, unusual architecture for VP55 that comprises of N-terminal, central or, catalytic, and C-terminal domains with different topologies and that, differs from many polymerases, including the eukaryotic poly(A), polymerases. Residues in the active site of VP55, located between the, catalytic and C-terminal domains, make specific interactions with the, adenine of the ATP analog, establishing the molecular basis of ATP, recognition. VP55's concave surface docks the globular VP39. A model for, RNA primer binding that involves all three VP55 domains and VP39 is, proposed. The model supports biochemical evidence that VP39 functions as a, processivity factor by partially enclosing the RNA primer at the, heterodimer interface.
About this Structure
2GA9 is a Protein complex structure of sequences from Vaccinia virus with CA and SAP as ligands. Active as mRNA (nucleoside-2'-O-)-methyltransferase, with EC number 2.1.1.57 Full crystallographic information is available from OCA.
Reference
Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity., Moure CM, Bowman BR, Gershon PD, Quiocho FA, Mol Cell. 2006 May 5;22(3):339-49. PMID:16678106
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