Structure Determination of Microtubules and Pili: Past, Present, and Future Directions

Frontiers in Molecular Biosciences

James A. Garnett¹  Joseph Atherton² 

[1] Centre for Host-Microbiome Interactions, Faculty of Dental, Oral and Craniofacial Sciences, King’s College London, London, United Kingdom;Randall Centre for Cell and Molecular Biophysics, King’s College London, London, United Kingdom;

关键词: cryo-EM;    ssNMR;    filament;    fibre;    microtubule;    pilus;   

DOI  :  10.3389/fmolb.2021.830304

来源: DOAJ

【 摘 要 】

Historically proteins that form highly polymeric and filamentous assemblies have been notoriously difficult to study using high resolution structural techniques. This has been due to several factors that include structural heterogeneity, their large molecular mass, and available yields. However, over the past decade we are now seeing a major shift towards atomic resolution insight and the study of more complex heterogenous samples and in situ/ex vivo examination of multi-subunit complexes. Although supported by developments in solid state nuclear magnetic resonance spectroscopy (ssNMR) and computational approaches, this has primarily been due to advances in cryogenic electron microscopy (cryo-EM). The study of eukaryotic microtubules and bacterial pili are good examples, and in this review, we will give an overview of the technical innovations that have enabled this transition and highlight the advancements that have been made for these two systems. Looking to the future we will also describe systems that remain difficult to study and where further technical breakthroughs are required.

【 授权许可】

Unknown