ArticleMolecular microbiology2012
Mechanism of the asymmetric activation of the MinD ATPase by MinE.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 68 citations in OpenAlex.
- Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation ineLife · 2026Article
- Article
- Recombinant TadZ from the type IVc pilus system induces protective immunity against virulentFrontiers in immunology · 2026Article
- Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation.Nature communications · 2025Article
- Tuning the interaction of a ParA-type ATPase with its partner separates bacterial organelle positioning from partitioning.Research square · 2025Article
- Tuning the interaction of a ParA-type ATPase with its partner separates bacterial organelle positioning from partitioning.bioRxiv : the preprint server for biology · 2025Article
- A programmable reaction-diffusion system for spatiotemporal cell signaling circuit design.Cell · 2024Article
- The mechanism of MinD stability modulation by MinE in Min protein dynamics.PLoS computational biology · 2023Article
- Septum site placement inMicrobiology (Reading, England) · 2023Article
- Multiple ParA/MinD ATPases coordinate the positioning of disparate cargos in a bacterial cell.Nature communications · 2023Article
- Distinct architectural requirements for theeLife · 2022Article
- Mass-sensitive particle tracking to elucidate the membrane-associated MinDE reaction cycle.Nature methods · 2021Article
- Dissection of the ATPase active site of McdA reveals the sequential steps essential for carboxysome distribution.Molecular biology of the cell · 2021Article
- CTP regulates membrane-binding activity of the nucleoid occlusion protein Noc.Molecular cell · 2021Article
- Article
- Architecture and regulation of an enterobacterial cellulose secretion system.Science advances · 2021Article
- C-terminal eYFP fusion impairsOpen biology · 2020Article
- The E. coli MinCDE system in the regulation of protein patterns and gradients.Cellular and molecular life sciences : CMLS · 2019Review
- Article
- The Min-protein oscillations inPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
MinD is a component of the Min system involved in the spatial regulation of cell division. It is an ATPase in the MinD/ParA/Mrp deviant Walker A motif family which is within the P loop GTPase superfamily. Its ATPase activity is stimulated by MinE; however, the mechanism of this activation is unclear. MinD forms a symmetric dimer with two binding sites for MinE; however, a recent model suggested that MinE occupying one site was sufficient for ATP hydrolysis. By generating heterodimers with one binding site for MinE we show that one binding site is sufficient for stimulation of the MinD ATPase. Furthermore, comparison of structures of MinD and related proteins led us to examine the role of N45 in the switch I region. An asparagine at this position is conserved in four of the deviant Walker A motif subfamilies (MinD, chromosomal ParAs, Get3 and FleN) and we find that N45 in MinD is essential for MinE-stimulated ATPase activity and suggest that it is a key residue affected by MinE binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.