Cryo‐EM structure of the MinCD copolymeric filament fromPseudomonas aeruginosaat 3.1 Å resolution
| Autor: | Andrzej Szewczak-Harris, J.M. Wagstaff, Jan Löwe |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
cell division
Models Molecular Cell division Protein Conformation Cryo-electron microscopy Biophysics macromolecular substances WACA medicine.disease_cause Biochemistry bacterial cytoskeleton Prokaryotic cytoskeleton Protein filament Membrane Lipids 03 medical and health sciences Bacterial Proteins Structural Biology Genetics medicine protein filaments FtsZ cryo‐EM Molecular Biology 030304 developmental biology computer.programming_language Adenosine Triphosphatases 0303 health sciences biology Chemistry Pseudomonas aeruginosa Cryoelectron Microscopy 030302 biochemistry & molecular biology Cell Biology Editor's Choice Cytoskeletal Proteins Membrane MINC Multiprotein Complexes biology.protein Protein Multimerization computer helical reconstruction |
| Zdroj: | Febs Letters |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1002/1873-3468.13471 |
| Popis: | Positioning of the division site in many bacterial species relies on the MinCDE system, which prevents the cytokinetic Z-ring from assembling anywhere but the mid-cell, through an oscillatory diffusion-reaction mechanism. MinD dimers bind to membranes and, via their partner MinC, inhibit the polymerization of cell division protein FtsZ into the Z-ring. MinC and MinD form polymeric assemblies in solution and on cell membranes. Here, we report the high-resolution cryo-EM structure of the copolymeric filaments of Pseudomonas aeruginosa MinCD. The filaments consist of three protofilaments made of alternating MinC and MinD dimers. The MinCD protofilaments are almost completely straight and assemble as single protofilaments on lipid membranes, which we also visualized by cryo-EM. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text