Bridging the N-terminal and middle domains in FliG of the flagellar rotor
Flagella are necessary for bacterial movement and contribute to various aspects of virulence. They are complex cylindrical structures built of multiple molecular rings with self-assembly properties. The flagellar rotor is composed of the MS-ring and the C-ring. The FliG protein of the C-ring is cent...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2022-01-01
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| Series: | Current Research in Structural Biology |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2665928X22000046 |
| _version_ | 1811292346500775936 |
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| author | Dagnija Tupiņa Alexander Krah Jan K. Marzinek Lorena Zuzic Adam A. Moverley Chrystala Constantinidou Peter J. Bond |
| author_facet | Dagnija Tupiņa Alexander Krah Jan K. Marzinek Lorena Zuzic Adam A. Moverley Chrystala Constantinidou Peter J. Bond |
| author_sort | Dagnija Tupiņa |
| collection | DOAJ |
| description | Flagella are necessary for bacterial movement and contribute to various aspects of virulence. They are complex cylindrical structures built of multiple molecular rings with self-assembly properties. The flagellar rotor is composed of the MS-ring and the C-ring. The FliG protein of the C-ring is central to flagellar assembly and function due to its roles in linking the C-ring with the MS-ring and in torque transmission from stator to rotor. No high-resolution structure of an assembled C-ring has been resolved to date, and the conformation adopted by FliG within the ring is unclear due to variations in available crystallographic data. Here, we use molecular dynamics (MD) simulations to study the conformation and dynamics of FliG in different states of assembly, including both in physiologically relevant and crystallographic lattice environments. We conclude that the linker between the FliG N-terminal and middle domain likely adopts an extended helical conformation in vivo, in contrast with the contracted conformation observed in some previous X-ray studies. We further support our findings with integrative model building of full-length FliG and a FliG ring model that is compatible with cryo-electron tomography (cryo-ET) and electron microscopy (EM) densities of the C-ring. Collectively, our study contributes to a better mechanistic understanding of the flagellar rotor assembly and its function. |
| first_indexed | 2024-04-13T04:44:03Z |
| format | Article |
| id | doaj.art-266646ab3ccb465bb454578b755e288b |
| institution | Directory Open Access Journal |
| issn | 2665-928X |
| language | English |
| last_indexed | 2024-04-13T04:44:03Z |
| publishDate | 2022-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Current Research in Structural Biology |
| spelling | doaj.art-266646ab3ccb465bb454578b755e288b2022-12-22T03:01:55ZengElsevierCurrent Research in Structural Biology2665-928X2022-01-0145967Bridging the N-terminal and middle domains in FliG of the flagellar rotorDagnija Tupiņa0Alexander Krah1Jan K. Marzinek2Lorena Zuzic3Adam A. Moverley4Chrystala Constantinidou5Peter J. Bond6Bioinformatics Institute, A∗STAR, 30 Biopolis Street, 138671, Singapore; Warwick Medical School, University of Warwick, Coventry, CV4 7AL, United KingdomBioinformatics Institute, A∗STAR, 30 Biopolis Street, 138671, SingaporeBioinformatics Institute, A∗STAR, 30 Biopolis Street, 138671, SingaporeBioinformatics Institute, A∗STAR, 30 Biopolis Street, 138671, Singapore; Department of Chemistry, Faculty of Science and Engineering, Manchester Institute of Biotechnology, The University of Manchester, Manchester, M1 7DN, United KingdomDepartment of Cell and Developmental Biology, University College London, London, WC1E 6BT, United KingdomWarwick Medical School, University of Warwick, Coventry, CV4 7AL, United KingdomBioinformatics Institute, A∗STAR, 30 Biopolis Street, 138671, Singapore; Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore; Corresponding author. Bioinformatics Institute, A∗STAR, 30 Biopolis Street, 138671, Singapore.Flagella are necessary for bacterial movement and contribute to various aspects of virulence. They are complex cylindrical structures built of multiple molecular rings with self-assembly properties. The flagellar rotor is composed of the MS-ring and the C-ring. The FliG protein of the C-ring is central to flagellar assembly and function due to its roles in linking the C-ring with the MS-ring and in torque transmission from stator to rotor. No high-resolution structure of an assembled C-ring has been resolved to date, and the conformation adopted by FliG within the ring is unclear due to variations in available crystallographic data. Here, we use molecular dynamics (MD) simulations to study the conformation and dynamics of FliG in different states of assembly, including both in physiologically relevant and crystallographic lattice environments. We conclude that the linker between the FliG N-terminal and middle domain likely adopts an extended helical conformation in vivo, in contrast with the contracted conformation observed in some previous X-ray studies. We further support our findings with integrative model building of full-length FliG and a FliG ring model that is compatible with cryo-electron tomography (cryo-ET) and electron microscopy (EM) densities of the C-ring. Collectively, our study contributes to a better mechanistic understanding of the flagellar rotor assembly and its function.http://www.sciencedirect.com/science/article/pii/S2665928X22000046 |
| spellingShingle | Dagnija Tupiņa Alexander Krah Jan K. Marzinek Lorena Zuzic Adam A. Moverley Chrystala Constantinidou Peter J. Bond Bridging the N-terminal and middle domains in FliG of the flagellar rotor Current Research in Structural Biology |
| title | Bridging the N-terminal and middle domains in FliG of the flagellar rotor |
| title_full | Bridging the N-terminal and middle domains in FliG of the flagellar rotor |
| title_fullStr | Bridging the N-terminal and middle domains in FliG of the flagellar rotor |
| title_full_unstemmed | Bridging the N-terminal and middle domains in FliG of the flagellar rotor |
| title_short | Bridging the N-terminal and middle domains in FliG of the flagellar rotor |
| title_sort | bridging the n terminal and middle domains in flig of the flagellar rotor |
| url | http://www.sciencedirect.com/science/article/pii/S2665928X22000046 |
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