TY - JOUR
T1 - Structure and Assembly of the Bacterial Flagellum
AU - Al-Otaibi, Natalie S.
AU - Bergeron, Julien R.C.
N1 - Publisher Copyright:
© 2022. The Author(s), under exclusive license to Springer Nature Switzerland AG.
PY - 2022/9/24
Y1 - 2022/9/24
N2 - The bacterial flagellum is a large macromolecular assembly that acts as propeller, providing motility through the rotation of a long extracellular filament. It is composed of over 20 different proteins, many of them highly oligomeric. Accordingly, it has attracted a huge amount of interest amongst researchers and the wider public alike. Nonetheless, most of its molecular details had long remained elusive.This however has changed recently, with the emergence of cryo-EM to determine the structure of protein assemblies at near-atomic resolution. Within a few years, the atomic details of most of the flagellar components have been elucidated, revealing not only its overall architecture but also the molecular details of its rotation mechanism. However, many questions remained unaddressed, notably on the complexity of the assembly of such an intricate machinery.In this chapter, we review the current state of our understanding of the bacterial flagellum structure, focusing on the recent development from cryo-EM. We also highlight the various elements that still remain to be fully characterized. Finally, we summarize the existing model for flagellum assembly and discuss some of the outstanding questions that are still pending in our understanding of the diversity of assembly pathways.
AB - The bacterial flagellum is a large macromolecular assembly that acts as propeller, providing motility through the rotation of a long extracellular filament. It is composed of over 20 different proteins, many of them highly oligomeric. Accordingly, it has attracted a huge amount of interest amongst researchers and the wider public alike. Nonetheless, most of its molecular details had long remained elusive.This however has changed recently, with the emergence of cryo-EM to determine the structure of protein assemblies at near-atomic resolution. Within a few years, the atomic details of most of the flagellar components have been elucidated, revealing not only its overall architecture but also the molecular details of its rotation mechanism. However, many questions remained unaddressed, notably on the complexity of the assembly of such an intricate machinery.In this chapter, we review the current state of our understanding of the bacterial flagellum structure, focusing on the recent development from cryo-EM. We also highlight the various elements that still remain to be fully characterized. Finally, we summarize the existing model for flagellum assembly and discuss some of the outstanding questions that are still pending in our understanding of the diversity of assembly pathways.
KW - Bacterial motility
KW - Bacterial secretion systems
KW - Cryo-EM
KW - Macromolecular structure
KW - Membrane proteins
UR - http://www.scopus.com/inward/record.url?scp=85138459290&partnerID=8YFLogxK
U2 - 10.1007/978-3-031-00793-4_13
DO - 10.1007/978-3-031-00793-4_13
M3 - Article
C2 - 36151384
AN - SCOPUS:85138459290
SN - 0306-0225
VL - 99
SP - 395
EP - 420
JO - Sub-Cellular Biochemistry
JF - Sub-Cellular Biochemistry
ER -