Structural Evolution of Bacterial Polyphosphate Degradation Enzyme for Phosphorus Cycling (Adv. Sci. 26/2024)

IF 14.3 1区材料科学 Q1 CHEMISTRY, MULTIDISCIPLINARY Advanced Science Pub Date : 2024-07-10 DOI:10.1002/advs.202470151

Shang Dai, Binqiang Wang, Rui Ye, Dong Zhang, Zhenming Xie, Ning Yu, Chunhui Cai, Cheng Huang, Jie Zhao, Furong Zhang, Yuejin Hua, Ye Zhao, Ruhong Zhou, Bing Tian

{"title":"Structural Evolution of Bacterial Polyphosphate Degradation Enzyme for Phosphorus Cycling (Adv. Sci. 26/2024)","authors":"Shang Dai, Binqiang Wang, Rui Ye, Dong Zhang, Zhenming Xie, Ning Yu, Chunhui Cai, Cheng Huang, Jie Zhao, Furong Zhang, Yuejin Hua, Ye Zhao, Ruhong Zhou, Bing Tian","doi":"10.1002/advs.202470151","DOIUrl":null,"url":null,"abstract":"<p><b>Linker-Based Structural Evolution</b></p><p>Phosphorus is a key element in the process of life origin. Polyphosphate is a phosphate “pool” in bacteria. In article number 2309602, Bing Tian, Ruhong Zhou, Shang Dai, and their co-workers demonstrate an interdomain linker-based exopolyphosphatase (PPX) structural evolution in bacteria. The length of α-linker in PPX, which involves phosphate cycling, is varied among bacteria and has impacts on protein's conformation and quaternary structure, thus poses an impact on enzyme activity and thermostability. The results suggest a potential relationship between PPX structural evolution and bacterial environmental adaptability, which shed light on enzymatic adaption for phosphorus cycling during natural evolution and rational design of the enzyme.\n\n <figure>\n <div><picture>\n <source></source></picture><p></p>\n </div>\n </figure></p>","PeriodicalId":117,"journal":{"name":"Advanced Science","volume":null,"pages":null},"PeriodicalIF":14.3000,"publicationDate":"2024-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/advs.202470151","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Advanced Science","FirstCategoryId":"88","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/advs.202470151","RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}

引用次数: 0

Abstract

Linker-Based Structural Evolution

Phosphorus is a key element in the process of life origin. Polyphosphate is a phosphate “pool” in bacteria. In article number 2309602, Bing Tian, Ruhong Zhou, Shang Dai, and their co-workers demonstrate an interdomain linker-based exopolyphosphatase (PPX) structural evolution in bacteria. The length of α-linker in PPX, which involves phosphate cycling, is varied among bacteria and has impacts on protein's conformation and quaternary structure, thus poses an impact on enzyme activity and thermostability. The results suggest a potential relationship between PPX structural evolution and bacterial environmental adaptability, which shed light on enzymatic adaption for phosphorus cycling during natural evolution and rational design of the enzyme.

Abstract Image

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

磷循环中细菌聚磷酸盐降解酶的结构进化（科学进展 26/2024）

基于连接体的结构进化磷是生命起源过程中的关键元素。聚磷酸盐是细菌中的磷酸盐 "池"。在文章编号2309602中，田兵、周如红、戴尚及其合作者展示了细菌中基于域间连接子的外聚磷酸酶（PPX）结构进化。PPX中涉及磷酸盐循环的α-连接体的长度在不同细菌中存在差异，并对蛋白质的构象和四元结构产生影响，从而对酶的活性和耐热性产生影响。研究结果表明，PPX 的结构进化与细菌的环境适应性之间存在潜在的关系，从而揭示了自然进化过程中酶对磷循环的适应性以及酶的合理设计。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

Advanced Science CHEMISTRY, MULTIDISCIPLINARYNANOSCIENCE &-NANOSCIENCE & NANOTECHNOLOGY

CiteScore

18.90

自引率

2.60%

发文量

1602

审稿时长

1.9 months

期刊介绍： Advanced Science is a prestigious open access journal that focuses on interdisciplinary research in materials science, physics, chemistry, medical and life sciences, and engineering. The journal aims to promote cutting-edge research by employing a rigorous and impartial review process. It is committed to presenting research articles with the highest quality production standards, ensuring maximum accessibility of top scientific findings. With its vibrant and innovative publication platform, Advanced Science seeks to revolutionize the dissemination and organization of scientific knowledge.