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首页> 外文期刊>Biochemistry >Structural Studies of AAV2 Rep68 Reveal a Partially Structured Linker and Compact Domain Conformation
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Structural Studies of AAV2 Rep68 Reveal a Partially Structured Linker and Compact Domain Conformation

机译：AAV2 Rep68的结构研究揭示了部分结构化的接头和紧凑的结构域构象

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摘要

Adeno-associated virus (AAV) nonstructural proteins Rep78 and Rep68 carry out all DNA transactions that regulate the AAV life cycle. They share two multifunctional domains: an N-terminal origin bindingicking domain (OBD) from the HUH superfamily and a SF3 helicase domain. A short linker of similar to 20 amino acids that is critical for oligomerization and function connects the two domains. Although X-ray structures of the AAV5 OBD and AAV2 helicase domains have been determined, information about the full-length protein and linker conformation is not known. This article presents the solution structure of AAV2 Rep68 using small-angle X-ray scattering (SAXS). We first determined the X-ray structures of the minimal AAV2 Rep68 OBD and of the OBD with the linker region. These X-ray structures reveal novel features that include a long C-terminal alpha-helix that protrudes from the core of the protein at a 45 degrees angle and a partially structured linker. SAXS studies corroborate that the linker is not extended, and we show that a praline residue in the linker is critical for Rep68 oligomerization and function. SAXS-based rigid-body modeling of Rep68 confirms these observations, showing a compact arrangement of the two domains in which they acquire a conformation that positions key residues in all domains on one face of the protein, poised to interact with DNA.
机译：腺相关病毒（AAV）非结构蛋白Rep78和Rep68进行所有调节AAV生命周期的DNA交易。它们共有两个多功能域：来自HUH超家族的N末端起源结合/切口域（OBD）和SF3解旋酶域。对寡聚和功能至关重要的类似于20个氨基酸的短连接子连接两个结构域。尽管已经确定了AAV5 OBD和AAV2解旋酶结构域的X射线结构，但有关全长蛋白质和接头构象的信息尚不清楚。本文介绍了使用小角度X射线散射（SAXS）的AAV2 Rep68的解决方案结构。我们首先确定了最小AAV2 Rep68 OBD和带有连接子区域的OBD的X射线结构。这些X射线结构揭示了新颖的特征，其中包括一个长的C端α螺旋，该螺旋以45度角从蛋白质的核心突出，并具有部分结构化的接头。 SAXS研究证实了该接头没有延伸，并且我们证明了该接头中的果仁糖残基对于Rep68寡聚化和功能至关重要。 Rep68的基于SAXS的刚体建模证实了这些观察结果，显示了两个域的紧凑排列，其中它们获得了一种构象，该构象将关键残基定位在蛋白质的所有域中，准备与DNA相互作用。

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