Crystal Structure of Thymidylate Synthase, Thy1, from Thermus thermophilus having an Extra C Terminal Domain

IF 0.9 4区 生物学
A. Ogawa, G. Sampei, G. Kawai
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引用次数: 0

Abstract

The thymidylate synthases ThyA and Thy1 are enzymes that catalyse the formation of thymidine monophosphate from 2′-deoxyuridine monophosphate. Thy1 (or ThyX) requires flavin for catalytic reactions, while ThyA does not. In the present study, the crystal structure of the flavin-dependent thymidylate synthase Thy1 from Thermus thermophilus HB8 (TtThy1, TTHA1096) was determined in complex with FAD and phosphate at 2.5 A resolution. TtThy1 is a tetrameric molecule like other Thy1 proteins, to which four FAD molecules are bound. In the crystal of TtThy1, two phosphate ions were bound to each dUMP-binding site. The characteristic feature of TtThy1 is the existence of an extra C-terminal domain (CTD) consisting of three α-helices and a β-strand. The function of the CTD is unknown and database analysis showed that this CTD is only shared by part of the Deinococcus–Thermus phylum.
具有额外C末端结构域的嗜热热菌胸腺酸合酶Thy1的晶体结构
胸腺苷酸合成酶ThyA和Thy1是催化2 ' -脱氧尿苷单磷酸形成胸腺苷单磷酸的酶。Thy1(或ThyX)需要黄素进行催化反应,而ThyA则不需要。在本研究中,从嗜热热菌HB8中提取的黄素依赖性胸苷酸合成酶Thy1 (TtThy1, TTHA1096)在2.5 A分辨率下与FAD和磷酸盐配合测定了晶体结构。TtThy1和其他Thy1蛋白一样是一个四聚体分子,与四个FAD分子结合。在TtThy1晶体中,两个磷酸离子分别与每个dump结合位点结合。TtThy1的特征是存在一个额外的c端结构域(CTD),由三个α-螺旋和一个β-链组成。CTD的功能尚不清楚,数据库分析表明,该CTD仅为部分热球菌门所共有。
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审稿时长
2-4 weeks
期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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