Structural model of a bacterial focal adhesion complex
Abstract Cell movement on surfaces relies on focal adhesion complexes (FAs), which connect cytoskeletal motors to the extracellular matrix to produce traction forces. The soil bacterium Myxococcus xanthus uses a bacterial FA (bFA), for surface movement and predation. The bFA system, known as Agl-Glt...
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| Format: | Article |
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Nature Portfolio
2025-01-01
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| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-025-07550-w |
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| author | Christian Cambillau Tâm Mignot |
| author_facet | Christian Cambillau Tâm Mignot |
| author_sort | Christian Cambillau |
| collection | DOAJ |
| description | Abstract Cell movement on surfaces relies on focal adhesion complexes (FAs), which connect cytoskeletal motors to the extracellular matrix to produce traction forces. The soil bacterium Myxococcus xanthus uses a bacterial FA (bFA), for surface movement and predation. The bFA system, known as Agl-Glt, is a complex network of at least 17 proteins spanning the cell envelope. Despite understanding the system dynamics, its molecular structure and protein interactions remain unclear. In this study, we utilize AlphaFold to generate models based on the known interactions and dynamics of gliding motility proteins. This approach provides us with a comprehensive view of the interactions across the entire complex. Our structural insights show the connection of essential functional modules throughout the cell envelope and offer an inspiring view of the force transduction mechanism from the inner molecular motor to the exterior of the cell. |
| format | Article |
| id | doaj-art-2eea7bf4ee314296aaca0a6f2656c00d |
| institution | Kabale University |
| issn | 2399-3642 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Communications Biology |
| spelling | doaj-art-2eea7bf4ee314296aaca0a6f2656c00d2025-01-26T12:48:18ZengNature PortfolioCommunications Biology2399-36422025-01-018111010.1038/s42003-025-07550-wStructural model of a bacterial focal adhesion complexChristian Cambillau0Tâm Mignot1Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IMM), Aix-Marseille Université—CNRS, UMR 7255Laboratoire de Chimie Bactérienne (LCB) Institut de Microbiologie, Bioénergies et Biotechnologie (IMM), Aix-Marseille Université—CNRS, UMR 7283Abstract Cell movement on surfaces relies on focal adhesion complexes (FAs), which connect cytoskeletal motors to the extracellular matrix to produce traction forces. The soil bacterium Myxococcus xanthus uses a bacterial FA (bFA), for surface movement and predation. The bFA system, known as Agl-Glt, is a complex network of at least 17 proteins spanning the cell envelope. Despite understanding the system dynamics, its molecular structure and protein interactions remain unclear. In this study, we utilize AlphaFold to generate models based on the known interactions and dynamics of gliding motility proteins. This approach provides us with a comprehensive view of the interactions across the entire complex. Our structural insights show the connection of essential functional modules throughout the cell envelope and offer an inspiring view of the force transduction mechanism from the inner molecular motor to the exterior of the cell.https://doi.org/10.1038/s42003-025-07550-w |
| spellingShingle | Christian Cambillau Tâm Mignot Structural model of a bacterial focal adhesion complex Communications Biology |
| title | Structural model of a bacterial focal adhesion complex |
| title_full | Structural model of a bacterial focal adhesion complex |
| title_fullStr | Structural model of a bacterial focal adhesion complex |
| title_full_unstemmed | Structural model of a bacterial focal adhesion complex |
| title_short | Structural model of a bacterial focal adhesion complex |
| title_sort | structural model of a bacterial focal adhesion complex |
| url | https://doi.org/10.1038/s42003-025-07550-w |
| work_keys_str_mv | AT christiancambillau structuralmodelofabacterialfocaladhesioncomplex AT tammignot structuralmodelofabacterialfocaladhesioncomplex |