Conformational Landscapes of a Class I Ribonucleotide Reductase Complex during Turnover Reveal Intrinsic Dynamics and Asymmetry

Author:

Xu DaORCID,Thomas William C.ORCID,Burnim Audrey A.ORCID,Ando NozomiORCID

Abstract

AbstractUnderstanding the structural dynamics associated with enzymatic catalysis has been a long-standing goal of structural biology. A wide range of motions, from small side-chain fluctuations to large domain rearrangements, have been implicated in enzyme function by experimental and computational studies. However, because structural techniques generally depend on averaging, direct visualization of conformational landscapes during turnover has been challenging. Here, we report the conformational landscapes of a class I ribonucleotide reductase (RNR) in various stages of turnover using single-particle cryo-electron microscopy (cryo-EM) and a combination of classification and deep-learning-based analyses. RNRs are responsible for the conversion of ribonucleotides to deoxyribonucleotides, a reaction that is essential for all DNA-based life. Class I RNRs, used by humans and other aerobic organisms, perform a complex series of chemical steps that are coupled with the dynamics of two highly mobile subunits, which can be resolved by EM. We demonstrate that despite the dimeric nature of the enzyme and its intrinsic dynamics, remarkable asymmetry is maintained across the class I RNR complex that physically segregates the two halves of its turnover cycle.

Publisher

Cold Spring Harbor Laboratory

Cited by 1 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3