SRP GTPase FlhF 的 GDP 结合态结构。

IF 1.1 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Acta crystallographica. Section F, Structural biology communications Pub Date : 2024-03-01 Epub Date: 2024-02-20 DOI:10.1107/S2053230X24000979

Anita Dornes, Christopher Nils Mais, Gert Bange

{"title":"SRP GTPase FlhF 的 GDP 结合态结构。","authors":"Anita Dornes, Christopher Nils Mais, Gert Bange","doi":"10.1107/S2053230X24000979","DOIUrl":null,"url":null,"abstract":"The GTPase FlhF, a signal recognition particle (SRP)-type enzyme, is pivotal for spatial-numerical control and bacterial flagella assembly across diverse species, including pathogens. This study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å. The structure exhibits the classical N- and G-domain fold, consistent with related SRP GTPases such as Ffh and FtsY. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis. These topological reconfigurations are similarly evident in Ffh and FtsY, and play a pivotal role in regulating the functions of these hydrolases.","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":"53-58"},"PeriodicalIF":1.1000,"publicationDate":"2024-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10910532/pdf/","citationCount":"0","resultStr":"{\"title\":\"Structure of the GDP-bound state of the SRP GTPase FlhF.\",\"authors\":\"Anita Dornes, Christopher Nils Mais, Gert Bange\",\"doi\":\"10.1107/S2053230X24000979\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The GTPase FlhF, a signal recognition particle (SRP)-type enzyme, is pivotal for spatial-numerical control and bacterial flagella assembly across diverse species, including pathogens. This study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å. The structure exhibits the classical N- and G-domain fold, consistent with related SRP GTPases such as Ffh and FtsY. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis. These topological reconfigurations are similarly evident in Ffh and FtsY, and play a pivotal role in regulating the functions of these hydrolases.\",\"PeriodicalId\":7029,\"journal\":{\"name\":\"Acta crystallographica. Section F, Structural biology communications\",\"volume\":\" \",\"pages\":\"53-58\"},\"PeriodicalIF\":1.1000,\"publicationDate\":\"2024-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10910532/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta crystallographica. Section F, Structural biology communications\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1107/S2053230X24000979\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/2/20 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta crystallographica. Section F, Structural biology communications","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1107/S2053230X24000979","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/2/20 0:00:00","PubModel":"Epub","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}

引用次数: 0

摘要

GTP酶FlhF是一种信号识别颗粒（SRP）型酶，在包括病原体在内的不同物种的空间-数量控制和细菌鞭毛组装中起着关键作用。本研究以 2.28 Å 的分辨率展示了 FlhF 在 GDP 结合态下的 X 射线结构。该结构表现出经典的 N 和 G 域折叠，与 Ffh 和 FtsY 等相关 SRP GTP 酶一致。与加载了 GTP 的 FlhF 的比较分析阐明了与 GTP 水解相关的构象变化。这些拓扑重组在 Ffh 和 FtsY 中同样明显，并在调节这些水解酶的功能方面发挥了关键作用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Structure of the GDP-bound state of the SRP GTPase FlhF.

查看原文本刊更多论文

Structure of the GDP-bound state of the SRP GTPase FlhF.

The GTPase FlhF, a signal recognition particle (SRP)-type enzyme, is pivotal for spatial-numerical control and bacterial flagella assembly across diverse species, including pathogens. This study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å. The structure exhibits the classical N- and G-domain fold, consistent with related SRP GTPases such as Ffh and FtsY. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis. These topological reconfigurations are similarly evident in Ffh and FtsY, and play a pivotal role in regulating the functions of these hydrolases.

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

Acta crystallographica. Section F, Structural biology communications BIOCHEMICAL RESEARCH METHODSBIOCHEMISTRY &-BIOCHEMISTRY & MOLECULAR BIOLOGY

CiteScore

1.90

自引率

0.00%

发文量

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.