4V02
MinC:MinD cell division protein complex, Aquifex aeolicus
Summary for 4V02
| Entry DOI | 10.2210/pdb4v02/pdb |
| Related | 4V03 |
| Descriptor | SITE-DETERMINING PROTEIN, PROBABLE SEPTUM SITE-DETERMINING PROTEIN MINC, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | cell cycle, bacterial cell division, ftsz, min system |
| Biological source | AQUIFEX AEOLICUS More |
| Total number of polymer chains | 4 |
| Total formula weight | 86608.45 |
| Authors | Ghosal, D.,Lowe, J. (deposition date: 2014-09-10, release date: 2015-01-14, Last modification date: 2024-05-08) |
| Primary citation | Ghosal, D.,Trambaiolo, D.,Amos, L.A.,Lowe, J. Mincd Cell Division Proteins Form Alternating Copolymeric Cytomotive Filaments. Nat.Commun., 5:5341-, 2014 Cited by PubMed Abstract: During bacterial cell division, filaments of the tubulin-like protein FtsZ assemble at midcell to form the cytokinetic Z-ring. Its positioning is regulated by the oscillation of MinCDE proteins. MinC is activated by MinD through an unknown mechanism and prevents Z-ring assembly anywhere but midcell. Here, using X-ray crystallography, electron microscopy and in vivo analyses, we show that MinD activates MinC by forming a new class of alternating copolymeric filaments that show similarity to eukaryotic septin filaments. A non-polymerizing mutation in MinD causes aberrant cell division in Escherichia coli. MinCD copolymers bind to membrane, interact with FtsZ and are disassembled by MinE. Imaging a functional msfGFP-MinC fusion protein in MinE-deleted cells reveals filamentous structures. EM imaging of our reconstitution of the MinCD-FtsZ interaction on liposome surfaces reveals a plausible mechanism for regulation of FtsZ ring assembly by MinCD copolymers. PubMed: 25500731DOI: 10.1038/NCOMMS6341 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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