ArticleNucleic acids research2019
Structures of maintenance of carboxysome distribution Walker-box McdA and McdB adaptor homologs.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- Article
- Brownian ratchet mechanisms for carboxysome positioning in bacteria.Current opinion in microbiology · 2025Review
- Organizing organelles: bacterial strategies for localizing intracellular compartments.Current opinion in microbiology · 2025Review
- Positioning of cellular components by the ParA/MinD family of ATPases.Current opinion in microbiology · 2024Review
- Dissecting the phase separation and oligomerization activities of the carboxysome positioning protein McdB.eLife · 2023Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- Dissection of the ATPase active site of McdA reveals the sequential steps essential for carboxysome distribution.Molecular biology of the cell · 2021Article
- The McdAB system positions α-carboxysomes in proteobacteria.Molecular microbiology · 2021Article
- Review
- Origin and Evolution of Carboxysome Positioning Systems in Cyanobacteria.Molecular biology and evolution · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Carboxysomes, protein-coated organelles in cyanobacteria, are important in global carbon fixation. However, these organelles are present at low copy in each cell and hence must be segregated to ensure transmission from one generation to the next. Recent studies revealed that a DNA partition-like ParA-ParB system mediates carboxysome maintenance, called McdA-McdB. Here, we describe the first McdA and McdB homolog structures. McdA is similar to partition ParA Walker-box proteins, but lacks the P-loop signature lysine involved in ATP binding. Strikingly, a McdA-ATP structure shows that a lysine distant from the P-loop and conserved in McdA homologs, enables ATP-dependent nucleotide sandwich dimer formation. Similar to partition ParA proteins this ATP-bound form binds nonspecific-DNA. McdB, which we show directly binds McdA, harbors a unique fold and appears to form higher-order oligomers like partition ParB proteins. Thus, our data reveal a new signature motif that enables McdA dimer formation and indicates that, similar to DNA segregation, carboxysome maintenance systems employ Walker-box proteins as DNA-binding motors while McdB proteins form higher order oligomers, which could function as adaptors to link carboxysomes and provide for stable transport by the McdA proteins.
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Registered trials
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