PLoS ONEBiochemistryPeer-reviewed journal article
Investigating the quaternary structure of a homomultimeric catechol 1,2-dioxygenase: An integrative structural biology study.
Arisbeth Guadalupe Almeida-Juarez, Shirish ChodankariD, Liliana Pardo‐LópeziD, Guadalupe Trinidad Zavala-Padilla, Enrique Rudiño-PiñeraiD
Abstract
The structural analysis of catechol 1,2 dioxygenase from Stutzerimonas frequens GOM2, SfC12DO, was conducted using various structural techniques. SEC-SAXS experiments revealed that SfC12DO, after lyophilization and reconstitution processes, can form multiple enzymatically active oligomers, including dimers, tetramers, and octamers. These findings differ from previous studies, which reported active dimers in homologous counterparts with available crystallographic structures, or trimers observed exclusively in solution for SfsC12DO and its homologous isoA C12DO from Acinetobacter radioresistens under low ionic strength conditions. In some cases, tetramers were also reported, such as for the Rodococcus erythropolis C12DO. The combined results of Small-Angle X-ray Scattering, Dynamic Light Scattering, and Transmission Electron Microscopy experiments provided additional insights into these active oligomers shape and molecular organization in an aqueous solution. These results highlight the oligomeric structural plasticity of SfC12DO, proving that it can exist in different oligomeric forms depending on the physicochemical characteristics of the solutions in which the experiments were performed. Remarkably, regardless of its oligomeric state, SfC12DO maintains its enzymatic activity even after prior lyophilization. All these characteristics make SfC12DO a very promising candidate for extensive bioremediation applications in polluted soils or waters.
- Citations
- 1
- FWCI
- 0.20
- Field percentile
- 31th percentile
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- The role of evolutionarily metastable oligomeric states in the optimization of catalytic activity
N. J. East, B. E. Clifton, … J. A. Kaczmarski·bioRxiv·Sep 13, 2022
- Divergent interactions maintain the quaternary octameric structure of a new family of esterases
Onit Alalouf, Rachel Salama, … Yuval Shoham·bioRxiv·Nov 19, 2018
- Structural characterization of covalently stabilized human cystatin C oligomers
M. Chrabaszczewska, A. K. Sieradzan, … M. Kozak·bioRxiv·Jul 27, 2020
- Deciphering the Cofilin Oligomers via Intermolecular Disulfide Bond Formation: A Coarse-grained Molecular Dynamics Approach to Understanding Cofilin's Regulation on Actin Filaments
C. Li, T. Wei, … M.-Y. Tsai·bioRxiv·Dec 7, 2023
- Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase, PmScsC
E. J. Furlong, F. Kurth, … J. L. Martin·bioRxiv·Sep 19, 2018
- Crystallographic and cryogenic electron microscopic structures and enzymatic characterization of sulfur oxygenase reductase from Sulfurisphaera tokodaii