4V03

MinD cell division protein, Aquifex aeolicus

Summary for 4V03

• Entry DOI: 10.2210/pdb4v03/pdb
• Related: 4V02
• Descriptor: SITE-DETERMINING PROTEIN, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: cell cycle, bacterial cell division, ftsz, min system
• Biological source: AQUIFEX AEOLICUS
• Total number of polymer chains: 2
• Total formula weight: 58127.61

Authors

Trambaiolo, 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

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: 25500731
DOI: 10.1038/NCOMMS6341

Experimental method

X-RAY DIFFRACTION (1.9 Å)