Evidence map›Paper›PMID 42234821›Full record

ArticlePlant physiology2026

"Air-Lock" gating mechanism of CsoS1D for metabolite translocation through the α-carboxysome shell.

Quan Wen, Yue Wang, Guo-Can Huang, Hong-Yu Pan, Yue-Yang Tang, Li-Hua Bie, Lu-Ning Liu, Jun Gao

Abstract read
In one paragraph

Article in Plant physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Quan WenHubei Key Laboratory of Agricultural Bioinformatics, College of Informatics, Huazhong Agricultural University, Wuhan 430070, China.ORCID 0009-0003-7575-5635
Yue WangHubei Key Laboratory of Agricultural Bioinformatics, College of Informatics, Huazhong Agricultural University, Wuhan 430070, China.ORCID 0009-0006-4813-2389
Guo-Can HuangHubei Key Laboratory of Agricultural Bioinformatics, College of Informatics, Huazhong Agricultural University, Wuhan 430070, China.ORCID 0009-0002-4842-2459
Hong-Yu PanHubei Key Laboratory of Agricultural Bioinformatics, College of Informatics, Huazhong Agricultural University, Wuhan 430070, China.ORCID 0009-0000-5347-2165
Yue-Yang TangInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom.
Li-Hua BieHubei Key Laboratory of Agricultural Bioinformatics, College of Informatics, Huazhong Agricultural University, Wuhan 430070, China.ORCID 0000-0002-3334-493X
Lu-Ning LiuHubei Key Laboratory of Agricultural Bioinformatics, College of Informatics, Huazhong Agricultural University, Wuhan 430070, China.ORCID 0000-0002-8884-4819
Jun GaoHubei Key Laboratory of Agricultural Bioinformatics, College of Informatics, Huazhong Agricultural University, Wuhan 430070, China.ORCID 0000-0002-6692-1828

Funding

Biotechnology and Biological Sciences Research Council BB/V009729/1Biotechnology and Biological Sciences Research Council BB/Y008308/1Biotechnology and Biological Sciences Research Council BB/Y01135X/1Central Universities 2662023XXPY006Central Universities 2662024XXPY003Leverhulme Trust RPG-2021-286National Natural Science Foundation of China 21873034Natural Environment Research Council NE/Z00019X/1University of Liverpool-China Scholarship Council
6 · The paper itself

Abstract

Carboxysomes are specialized bacterial microcompartments (BMCs) for CO2 assimilation in cyanobacteria and many chemoautotrophs. Selective transport of gas molecules and metabolites across the carboxysome shell plays an essential role in creating a high-CO2 environment around Rubisco and ensuring efficient metabolite flux. However, the molecular mechanisms underlying this specific permeability remain elusive. Using integrated computational approaches, including all-atom molecular dynamics (MD) simulations, self-random acceleration MD simulations, umbrella sampling and targeted MD simulations, we systematically investigated the permeation pathways of large anionic metabolites ribulose-1,5-bisphosphate (RuBP) and 3-phosphoglycerate (3-PGA) through the α-carboxysome shell protein CsoS1D, which exhibits a trimer-of-dimer architecture and an enlarged central pore compared with hexameric and pentameric shell proteins. The results indicate that the central pore of CsoS1D serves as the primary conduit for the translocation of bulky metabolites RuBP and 3-PGA and reveal a 3-stage "air-lock" transport mechanism driven by electrostatic interactions. Moreover, the shallow free-energy landscape for channel gating enables the pore to undergo frequent, thermally driven transitions between open and closed states, implementing a conformational selection transport model independent of ligand binding. Our analysis further revealed 5 conserved residues that establish an electrostatic transport pathway within trimeric shell proteins, suggesting that this permeability mechanism represents a generalizable design principle across diverse BMCs. By elucidating shell protein permeability mechanisms at atomic resolution, this study lays the framework for understanding carboxysome physiology and guides the rational engineering of carboxysome permeability to facilitate system-level metabolic modeling and optimization of synthetic carboxysomes for biotechnological applications.

Indexed as

Bacterial ProteinsBiological TransportGlyceric AcidsMolecular Dynamics SimulationRibulosephosphates3-phosphoglycerateBacterial ProteinsGlyceric AcidsRibulosephosphates

Identifiers

PMID42234821
PMCPMC13316943

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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.