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[[Image:2gaf.gif|left|200px]]
{{Seed}}
[[Image:2gaf.png|left|200px]]


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{{STRUCTURE_2gaf|  PDB=2gaf  |  SCENE=  }}  
{{STRUCTURE_2gaf|  PDB=2gaf  |  SCENE=  }}  


'''Crystal Structure of the Vaccinia Polyadenylate Polymerase Heterodimer (apo form)'''
===Crystal Structure of the Vaccinia Polyadenylate Polymerase Heterodimer (apo form)===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Pox virus]]
[[Category: Pox virus]]
[[Category: Processivity]]
[[Category: Processivity]]
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Revision as of 14:49, 27 July 2008

File:2gaf.png

Template:STRUCTURE 2gaf

Crystal Structure of the Vaccinia Polyadenylate Polymerase Heterodimer (apo form)

Template:ABSTRACT PUBMED 16678106

About this Structure

2GAF is a Protein complex structure of sequences from Vaccinia virus. 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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