2GA9

Crystal Structure of the Heterodimeric Vaccinia Virus Polyadenylate Polymerase with Bound ATP-gamma-S

2GA9 の概要

• エントリーDOI: 10.2210/pdb2ga9/pdb
• 分子名称: Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase, Poly(A) polymerase catalytic subunit, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: polyadenylate polymerase, nucleotidyltransferase, poxvirus, heterodimer, processivity, transferase
• 由来する生物種: Vaccinia virus; 詳細
• 細胞内の位置: Virion : P07617
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90104.46

構造登録者

Moure, C.M.,Bowman, B.R.,Gershon, P.D.,Quiocho, F.A. (登録日: 2006-03-08, 公開日: 2006-05-16, 最終更新日: 2024-02-14)

主引用文献

Moure, C.M.,Bowman, B.R.,Gershon, P.D.,Quiocho, F.A.
Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity.
Mol.Cell, 22:339-349, 2006

PubMed Abstract: 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.

PubMed: 16678106
DOI: 10.1016/j.molcel.2006.03.015

実験手法

X-RAY DIFFRACTION (2.3 Å)