Structural basis of assembly and torque transmission of the bacterial flagellar motor

Tan, James S.; Zhang, Xing; Wang, Xiaofei; Xu, Chenchao; Chang, Shenghai; Wu, Haixiao; Wang, Ting; Liang, Huihui; Gao, Haichun; Zhou, Yan; Zhu, Yongqun

doi:10.1016/j.cell.2021.03.057

Cited by 91 publications

(103 citation statements)

References 67 publications

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“…The structure of the FliE within the intact flagellar basal body has recently been solved ( Fig. 1 ) ( 18 , 19 ). This allows us to assess how the fliE mutants and the extragenic suppressors described in this study might affect the function of FliE as an adaptor between the core fT3SS, the FliF MS-ring, and the proximal rod component of the basal body.…”

Section: Discussionmentioning

confidence: 99%

“…FliE consists of three α-helices, α1, α2, and α3 ( Fig. 6 ) ( 18 , 19 ). The α1 helix binds to the inner wall of the MS-ring.…”

Section: Discussionmentioning

confidence: 99%

“…6B ) ( 13 ). Domain D0 formed by α2 and α3 helices of FliE binds to FliP and FliR and induces helical rearrangements of the protein export channel, resulting in an open conformation of the exit gate ( 18 , 19 ). Ala-95 and Val-99 of FliE make a hydrophobic contact with Pro-55 of FliP ( Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The basal body is composed of the MS-ring (FliF), C-ring (FliG, FliM, and FliN), P-ring (FlgI), L-ring (FlgH), and rod (FliE, FlgB, FlgC, FlgE, and FlgG). The cryoEM structure for the basal structure, including the MS-ring, rod, and PL-ring, has recently been solved ( 18 , 19 ), as has the FliP 5 FliQ 4 FliR core secretion complex ( 13 ). The flagellar type III secretion system (fT3SS) is located at the flagellar base and transports flagellar building blocks such as rod proteins from the cytoplasm to the distal end of the growing flagellar structure.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, the Salmonella basal body structure has been solved by cryoelectron microscopy (cryoEM) image analysis ( Fig. 1 ) ( 18 , 19 ). Six copies of FliE assemble into the most proximal part of the rod in the MS-ring.…”

Section: Introductionmentioning

confidence: 99%

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Genetic Analysis of the Salmonella FliE Protein That Forms the Base of the Flagellar Axial Structure

Hendriksen

Lee

Bradshaw

et al. 2021

mBio

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The FliE component of the bacterial flagellum is the first protein secreted through the flagellar type III secretion system (fT3SS) that is capable of self-assembly into the growing bacterial organelle. The FliE protein plays dual roles in the assembly of the Salmonella flagellum as the final component of the flagellar type III secretion system (fT3SS) and as an adaptor protein that anchors the rod (drive shaft) of the flagellar motor to the membrane-imbedded MS-ring structure.

show abstract

Section: Discussionmentioning

confidence: 99%

“…FliE consists of three α-helices, α1, α2, and α3 ( Fig. 6 ) ( 18 , 19 ). The α1 helix binds to the inner wall of the MS-ring.…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Genetic Analysis of the Salmonella FliE Protein That Forms the Base of the Flagellar Axial Structure

Hendriksen

Lee

Bradshaw

et al. 2021

mBio

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Flagella of Tumor‐Targeting Bacteria Trigger Local Hemorrhage to Reprogram Tumor‐Associated Macrophages for Improved Antitumor Therapy

Xiong

Chen

et al. 2023

Advanced Materials

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Tumor‐associated macrophages (TAMs) exhibit an immunosuppressive M2 phenotype and lead to failure of antitumor therapy. Infiltrated erythrocytes during hemorrhage are recognized as a promising strategy for polarizing TAMs. However, novel materials that precisely induce tumor hemorrhage without affecting normal coagulation still face challenges. Here, tumor‐targeting bacteria (flhDC VNP) are genetically constructed to realize precise tumor hemorrhage. FlhDC VNP colonizes the tumor and overexpresses flagella during proliferation. The flagella promote the expression of tumor necrosis factor α, which induces local tumor hemorrhage. Infiltrated erythrocytes during the hemorrhage temporarily polarize macrophages to the M1 subtype. In the presence of artesunate, this short‐lived polarization is transformed into a sustained polarization because artesunate and heme form a complex that continuously produces reactive oxygen species. Therefore, the flagella of active tumor‐targeting bacteria may open up new strategies for reprogramming TAMs and improving antitumor therapy.

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Assessment of the CASP14 assembly predictions

2021

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In CASP14, 39 research groups submitted more than 2500 3D models on 22 protein complexes. In general, the community performed well in predicting the fold of the assemblies (for 80% of the targets), although it faced significant challenges in reproducing the native contacts. This is especially the case for the complexes without whole-assembly templates. The leading predictor, BAKER-experimental, used a methodology combining classical techniques (template-based modeling, protein docking) with deep learning-based contact predictions and a fold-and-dock approach. The Venclovas team achieved the runner-up position with template-based modeling and docking. By analyzing the target interfaces, we showed that the complexes with depleted charged contacts or dominating hydrophobic interactions were the most challenging ones to predict. We also demonstrated that if AlphaFold2 predictions were at hand, the interface prediction challenge could be alleviated for most of the targets. All in all, it is evident that new approaches are needed for the accurate prediction of assemblies, which undoubtedly will expand on the significant improvements in the tertiary structure prediction field.

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Structural basis of assembly and torque transmission of the bacterial flagellar motor

Cited by 91 publications

References 67 publications

Genetic Analysis of the Salmonella FliE Protein That Forms the Base of the Flagellar Axial Structure

Genetic Analysis of the Salmonella FliE Protein That Forms the Base of the Flagellar Axial Structure

Flagella of Tumor‐Targeting Bacteria Trigger Local Hemorrhage to Reprogram Tumor‐Associated Macrophages for Improved Antitumor Therapy

Assessment of the CASP14 assembly predictions

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