TY - JOUR
T1 - Cryo-EM of the injectisome and type III secretion systems
AU - Bergeron, Julien R.C.
AU - Marlovits, Thomas C.
N1 - Funding Information:
This work was funded by grants from the BBSRC ( BB/R009759/2 ) and HFSP ( RGY0080 /2021 ) to JRCB, and by funds available to TCM through the Behörde für Wissenschaft, Forschung und Gleichstellung of the city of Hamburg at the Institute of Structural and Systems Biology at the University Medical Center Hamburg–Eppendorf (UKE), and Deutsches Elektronen Synchrotron (DESY).
Publisher Copyright:
© 2022 The Author(s)
PY - 2022/8
Y1 - 2022/8
N2 - Double-membrane-spanning protein complexes, such as the T3SS, had long presented an intractable challenge for structural biology. As a consequence, until a few years ago, our molecular understanding of this fascinating complex was limited to composite models, consisting of structures of isolated domains, positioned within the overall complex. Most of the membrane-embedded components remained completely uncharacterized. In recent years, the emergence of cryo-electron microscopy (cryo-EM) as a method for determining protein structures to high resolution, has be transformative to our capacity to understand the architecture of this complex, and its mechanism of substrate transport. In this review, we summarize the recent structures of the various T3SS components, determined by cryo-EM, and highlight the regions of the complex that remain to be characterized. We also discuss the recent structural insights into the mechanism of effector transport through the T3SS. Finally, we highlight some of the challenges that remain to be tackled.
AB - Double-membrane-spanning protein complexes, such as the T3SS, had long presented an intractable challenge for structural biology. As a consequence, until a few years ago, our molecular understanding of this fascinating complex was limited to composite models, consisting of structures of isolated domains, positioned within the overall complex. Most of the membrane-embedded components remained completely uncharacterized. In recent years, the emergence of cryo-electron microscopy (cryo-EM) as a method for determining protein structures to high resolution, has be transformative to our capacity to understand the architecture of this complex, and its mechanism of substrate transport. In this review, we summarize the recent structures of the various T3SS components, determined by cryo-EM, and highlight the regions of the complex that remain to be characterized. We also discuss the recent structural insights into the mechanism of effector transport through the T3SS. Finally, we highlight some of the challenges that remain to be tackled.
UR - http://www.scopus.com/inward/record.url?scp=85132215946&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2022.102403
DO - 10.1016/j.sbi.2022.102403
M3 - Review article
AN - SCOPUS:85132215946
SN - 0959-440X
VL - 75
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
M1 - 102403
ER -