Open and Hybridized: The Topology of Chloroplast Barrel Proteins
- 1University of Kansas
Abstract
Despite their central role in metabolite exchange, lipid trafficking, and protein import, chloroplast outer envelope beta-barrel proteins lack a dedicated comprehensive sequence database spanning many plant proteomes. Here we present the database COB (chloroplast outer-envelope beta-barrel), consisting of 16,586 beta-barrel sequences which we organize across ten protein categories and an uncharacterized group. COB was constructed using a machine learning classifier that identifies chloroplast beta-barrels based on features derived from evolutionary protein contact maps. Analysis of COB reveals that Streptophyta have more barrels overall and use a greater variety of solute transporters than Chlorophyta. Furthermore, we find considerable structural diversity across OEP categories, including variation in beta-strand count and a high prevalence of open barrel conformations not observed in bacterial outer membrane proteins. Structure predictions for Arabidopsis thaliana outer envelope proteins identified candidate hybrid barrel assemblies, with TOC159 family members emerging as universal interaction partners. We also report single-chain multi-barrel domain architectures in the chloroplast outer envelope, a topology previously described only in Gram-negative bacteria. Finally, we find chloroplast membrane barrels have more open topologies and shorter strands than bacterial membrane barrels. COB provides a comprehensive sequence resource for chloroplast outer envelope beta-barrels and establishes a foundation for investigating the evolution, structure, and function of the chloroplast outer envelope.
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BibTeX
@misc{proctor2026open,
title = {{Open and Hybridized: The Topology of Chloroplast Barrel Proteins}},
author = {E. Proctor and D. Montezano and M. M. Copeland and J. S. G. Slusky},
howpublished = {bioRxiv},
year = {2026},
month = jul,
doi = {10.64898/2026.07.15.738633},
url = {https://www.biorxiv.org/content/10.64898/2026.07.15.738633v2},
note = {CC BY-ND},
}
RIS
TY - UNPB
TI - Open and Hybridized: The Topology of Chloroplast Barrel Proteins
AU - E. Proctor
AU - D. Montezano
AU - M. M. Copeland
AU - J. S. G. Slusky
PY - 2026
DA - 2026/07/15
PB - bioRxiv
DO - 10.64898/2026.07.15.738633
UR - https://www.biorxiv.org/content/10.64898/2026.07.15.738633v2
AB - Despite their central role in metabolite exchange, lipid trafficking, and protein import, chloroplast outer envelope beta-barrel proteins lack a dedicated comprehensive sequence database spanning many plant proteomes. Here we present the database COB (chloroplast outer-envelope beta-barrel), consisting of 16,586 beta-barrel sequences which we organize across ten protein categories and an uncharacterized group. COB was constructed using a machine learning classifier that identifies chloroplast beta-barrels based on features derived from evolutionary protein contact maps. Analysis of COB reveals that Streptophyta have more barrels overall and use a greater variety of solute transporters than Chlorophyta. Furthermore, we find considerable structural diversity across OEP categories, including variation in beta-strand count and a high prevalence of open barrel conformations not observed in bacterial outer membrane proteins. Structure predictions for Arabidopsis thaliana outer envelope proteins identified candidate hybrid barrel assemblies, with TOC159 family members emerging as universal interaction partners. We also report single-chain multi-barrel domain architectures in the chloroplast outer envelope, a topology previously described only in Gram-negative bacteria. Finally, we find chloroplast membrane barrels have more open topologies and shorter strands than bacterial membrane barrels. COB provides a comprehensive sequence resource for chloroplast outer envelope beta-barrels and establishes a foundation for investigating the evolution, structure, and function of the chloroplast outer envelope.
ER -