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首页> 外文期刊>EMBO Journal >The structure of a protein primer-polymerase complex in the initiation of genome replication
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The structure of a protein primer-polymerase complex in the initiation of genome replication

机译：primer-polymerase蛋白质的结构复杂的基因组复制的起始

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摘要

Picornavirus RNA replication is initiated by the covalent attachment of a UMP molecule to the hydroxyl group of a tyrosine in the terminal protein VPg. This reaction is carried out by the viral RNA- dependent RNA polymerase ( 3D). Here, we report the X- ray structure of two complexes between foot- and- mouth disease virus 3D, VPg1, the substrate UTP and divalent cations, in the absence and in the presence of an oligoadenylate of 10 residues. In both complexes, VPg fits the RNA binding cleft of the polymerase and projects the key residue Tyr3 into the active site of 3D. This is achieved by multiple interactions with residues of motif F and helix alpha 8 of the fingers domain and helix alpha 13 of the thumb domain of the polymerase. The complex obtained in the presence of the oligoadenylate showed the product of the VPg uridylylation ( VPg- UMP). Two metal ions and the catalytic aspartic acids of the polymerase active site, together with the basic residues of motif F, have been identified as participating in the priming reaction.
机译：小核糖核酸病毒RNA复制是发起的人民运动联盟分子共价连接的在终端羟基的酪氨酸蛋白质VPg。依赖病毒RNA, RNA聚合酶(3 d)。我们报告两个配合物的X -射线结构脚- - - -口病病毒3 d, VPg1,衬底UTP和二价阳离子,在没有和oligoadenylate的存在10残留。核糖核酸绑定裂的聚合酶和项目关键Tyr3残留活性部位的3 d。这是通过多个交互残留的主题8 F和α螺旋手指域和α螺旋13的拇指域的聚合酶。oligoadenylate显示的存在产品VPg中uridylylation (VPg -运动联盟)。金属离子的催化天冬胺酸聚合酶活性部位,一起基本的主题F的残渣,已确定作为参与启动反应。

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