来自热球菌sp. 1519的atp依赖性DNA连接酶显示了OB-fold结构域的新排列。

T Petrova, E Y Bezsudnova, K M Boyko, A V Mardanov, K M Polyakov, V V Volkov, M Kozin, N V Ravin, I G Shabalin, K G Skryabin, T N Stekhanova, M V Kovalchuk, V O Popov
{"title":"来自热球菌sp. 1519的atp依赖性DNA连接酶显示了OB-fold结构域的新排列。","authors":"T Petrova,&nbsp;E Y Bezsudnova,&nbsp;K M Boyko,&nbsp;A V Mardanov,&nbsp;K M Polyakov,&nbsp;V V Volkov,&nbsp;M Kozin,&nbsp;N V Ravin,&nbsp;I G Shabalin,&nbsp;K G Skryabin,&nbsp;T N Stekhanova,&nbsp;M V Kovalchuk,&nbsp;V O Popov","doi":"10.1107/S1744309112043394","DOIUrl":null,"url":null,"abstract":"<p><p>DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl termini. Their function is essential for maintaining genome integrity in the replication, recombination and repair of DNA. High flexibility is important for the function of DNA ligase molecules. Two types of overall conformations of archaeal DNA ligase that depend on the relative position of the OB-fold domain have previously been revealed: closed and open extended conformations. The structure of ATP-dependent DNA ligase from Thermococcus sp. 1519 (LigTh1519) in the crystalline state determined at a resolution of 3.02 Å shows a new relative arrangement of the OB-fold domain which is intermediate between the positions of this domain in the closed and the open extended conformations of previously determined archaeal DNA ligases. However, small-angle X-ray scattering (SAXS) measurements indicate that in solution the LigTh1519 molecule adopts either an open extended conformation or both an intermediate and an open extended conformation with the open extended conformation being dominant.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":"68 Pt 12","pages":"1440-7"},"PeriodicalIF":0.9000,"publicationDate":"2012-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309112043394","citationCount":"15","resultStr":"{\"title\":\"ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.\",\"authors\":\"T Petrova,&nbsp;E Y Bezsudnova,&nbsp;K M Boyko,&nbsp;A V Mardanov,&nbsp;K M Polyakov,&nbsp;V V Volkov,&nbsp;M Kozin,&nbsp;N V Ravin,&nbsp;I G Shabalin,&nbsp;K G Skryabin,&nbsp;T N Stekhanova,&nbsp;M V Kovalchuk,&nbsp;V O Popov\",\"doi\":\"10.1107/S1744309112043394\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl termini. Their function is essential for maintaining genome integrity in the replication, recombination and repair of DNA. High flexibility is important for the function of DNA ligase molecules. Two types of overall conformations of archaeal DNA ligase that depend on the relative position of the OB-fold domain have previously been revealed: closed and open extended conformations. The structure of ATP-dependent DNA ligase from Thermococcus sp. 1519 (LigTh1519) in the crystalline state determined at a resolution of 3.02 Å shows a new relative arrangement of the OB-fold domain which is intermediate between the positions of this domain in the closed and the open extended conformations of previously determined archaeal DNA ligases. However, small-angle X-ray scattering (SAXS) measurements indicate that in solution the LigTh1519 molecule adopts either an open extended conformation or both an intermediate and an open extended conformation with the open extended conformation being dominant.</p>\",\"PeriodicalId\":7310,\"journal\":{\"name\":\"Acta Crystallographica Section F-structural Biology and Crystallization Communications\",\"volume\":\"68 Pt 12\",\"pages\":\"1440-7\"},\"PeriodicalIF\":0.9000,\"publicationDate\":\"2012-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1107/S1744309112043394\",\"citationCount\":\"15\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta Crystallographica Section F-structural Biology and Crystallization Communications\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1107/S1744309112043394\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2012/11/14 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1107/S1744309112043394","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2012/11/14 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 15

摘要

DNA连接酶通过催化在相邻的5'-磷酸和3'-羟基末端之间形成磷酸二酯键来连接双链DNA中的单链断裂。它们的功能对于在DNA的复制、重组和修复中保持基因组完整性至关重要。高柔性对于DNA连接酶分子的功能是重要的。古菌DNA连接酶的两种类型的整体构象取决于OB折叠结构域的相对位置:闭合构象和开放延伸构象。来自Thermococcus sp.1519(LigTh1519)的ATP依赖性DNA连接酶在结晶状态下的结构以3.02的分辨率测定 Å显示了OB折叠结构域的一种新的相对排列,它位于该结构域在先前确定的古菌DNA连接酶的闭合和开放延伸构象中的位置之间。然而,小角度X射线散射(SAXS)测量表明,在溶液中,LigTh1519分子要么采用开放延伸构象,要么采用中间体和开放延伸构象两者,其中开放延伸构象占主导地位。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

摘要图片

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.

DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl termini. Their function is essential for maintaining genome integrity in the replication, recombination and repair of DNA. High flexibility is important for the function of DNA ligase molecules. Two types of overall conformations of archaeal DNA ligase that depend on the relative position of the OB-fold domain have previously been revealed: closed and open extended conformations. The structure of ATP-dependent DNA ligase from Thermococcus sp. 1519 (LigTh1519) in the crystalline state determined at a resolution of 3.02 Å shows a new relative arrangement of the OB-fold domain which is intermediate between the positions of this domain in the closed and the open extended conformations of previously determined archaeal DNA ligases. However, small-angle X-ray scattering (SAXS) measurements indicate that in solution the LigTh1519 molecule adopts either an open extended conformation or both an intermediate and an open extended conformation with the open extended conformation being dominant.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
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.
期刊最新文献
Crystal Structure of Thymidylate Synthase, Thy1, from Thermus thermophilus having an Extra C Terminal Domain The dimerization domain of human SFPQ in space group C2221 A revisited version of the apo structure of the ligand-binding domain of the human nuclear receptor RXR-ALPHA INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN) with tetrabrachion (TB) domain stalk Glutathione reductase from Streptococcus pneumoniae
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1