Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G
Extensive mutagenesis experiments corroborate a structural model for the DNA deaminase domain of APOBEC3G
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DOI：
10.1016/j.febslet.2007.08.076
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发表时间：
2007-10-02
期刊：
影响因子：
3.5
通讯作者：
Harris, Reuben S.
中科院分区：
文献类型：
--
作者：
Chen, Kuan-Ming;Martemyanova, Natalia;Harris, Reuben S.
APOBEC3G 是一种单链 DNA 胞嘧啶脱氨酶，能够阻断逆转录病毒和逆转录转座子的复制。 APOBEC3G 有两个保守的锌配位基序，但催化只需要一个。此处，缺失分析显示最小催化结构域由残基 198-384 组成。尺寸排阻测定表明该蛋白质是单体的。 APOBEC3G198-384 的许多 (31169) 丙氨酸取代衍生物保留了显着至完全水平的活性。这些数据证实了 APOBEC3G 催化结构域的基于 APOBEC2 的结构模型，表明大多数非必需残基是溶剂可及的，并且大多数必需残基聚集在蛋白质核心内。 (c) 2007 年欧洲生化学会联合会。由 Elsevier B.V. 出版。保留所有权利。
APOBEC3G is a single-strand DNA cytosine deaminase capable of blocking retrovirus and retrotransposon replication. APOBEC3G has two conserved zinc-coordinating motifs but only one is required for catalysis. Here, deletion analyses revealed that the minimal catalytic domain consists of residues 198-384. Size exclusion assays indicated that this protein is monomeric. Many (31169) alanine substitution derivatives of APOBEC3G198-384 retained significant to full levels of activity. These data corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.