ArticleJournal of experimental botany2017
Crystal structures of β-carboxysome shell protein CcmP: ligand binding correlates with the closed or open central pore.
Article in Journal of experimental botany, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- From fundamental understanding to engineering of carboxysomes for biotechnological applications.Plant communications · 2026Review
- Overexpression of β-carboxysomes increases photosynthesis and growth in Synechocystis sp. PCC 6803.Plant physiology · 2026Article
- "Air-Lock" gating mechanism of CsoS1D for metabolite translocation through the α-carboxysome shell.Plant physiology · 2026Article
- Gas exchange measurements of carboxysome mutants reveal insights into cyanobacterial carbon-concentrating mechanisms.Plant physiology · 2026Article
- Recent insights into α-carboxysome structure, mechanism, and assembly.Journal of bacteriology · 2026Review
- Molecular Modeling and Molecular Dynamics Simulation of a Packed and Intact Bacterial Microcompartment.The journal of physical chemistry. B · 2025Article
- Understanding carboxysomes to enhance carbon fixation in crops.Biochemical Society transactions · 2025Review
- Rubisco packaging and stoichiometric composition of the native β-carboxysome in Synechococcus elongatus PCC7942.Plant physiology · 2024Article
- Electrochemical cofactor recycling of bacterial microcompartments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Characterization of a widespread sugar phosphate-processing bacterial microcompartment.Communications biology · 2024Article
- Atomic view of photosynthetic metabolite permeability pathways and confinement in synthetic carboxysome shells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular interactions of the chaperone CcmS and carboxysome shell protein CcmK1 that mediate β-carboxysome assembly.Plant physiology · 2024Article
- Article
- Rubisco packaging and stoichiometric composition of a native β-carboxysome.bioRxiv : the preprint server for biology · 2024Article
- Comparative Pore Structure and Dynamics for Bacterial Microcompartment Shell Protein Assemblies in Sheets or Shells.ACS omega · 2024Article
- Electrochemical cofactor recycling of bacterial microcompartments.bioRxiv : the preprint server for biology · 2024Article
- Comparative Pore Structure and Dynamics for Bacterial Microcompartment Shell Protein Assemblies in Sheets or Shells.bioRxiv : the preprint server for biology · 2024Article
- The primary carbon metabolism in cyanobacteria and its regulation.Frontiers in plant science · 2024Review
- Monatomic ions influence substrate permeation across bacterial microcompartment shells.Scientific reports · 2023Article
- Evolutionary relationships among shell proteins of carboxysomes and metabolosomes.Current opinion in microbiology · 2021Review
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Cyanobacterial CO2 fixation is promoted by encapsulating and co-localizing the CO2-fixing enzymes within a protein shell, the carboxysome. A key feature of the carboxysome is its ability to control selectively the flux of metabolites in and out of the shell. The β-carboxysome shell protein CcmP has been shown to form a double layer of pseudohexamers with a relatively large central pore (~13 Å diameter), which may allow passage of larger metabolites such as the substrate for CO2 fixation, ribulose 1,5-bisphosphate, through the shell. Here we describe two crystal structures, at 1.45 Å and 1.65 Å resolution, of CcmP from Synechococcus elongatus PCC7942 (SeCcmP). The central pore of CcmP is open or closed at its ends, depending on the conformation of two conserved residues, Glu69 and Arg70. The presence of glycerol resulted in a pore that is open at one end and closed at the opposite end. When glycerol was omitted, both ends of the barrel became closed. A binding pocket at the interior of the barrel featured residual density with distinct differences in size and shape depending on the conformation, open or closed, of the central pore of SeCcmP, suggestive of a metabolite-driven mechanism for the gating of the pore.
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