Structural basis of substrate progression through the bacterial chaperonin cycle
The bacterial chaperonin GroEL-GroES promotes protein folding through ATP-regulated
cycles of substrate protein binding, encapsulation, and release. Here, we have used cryoEM …
cycles of substrate protein binding, encapsulation, and release. Here, we have used cryoEM …
Temperature Regulates Stability, Ligand Binding (Mg2+ and ATP), and Stoichiometry of GroEL–GroES Complexes
Chaperonins are nanomachines that harness ATP hydrolysis to power and catalyze protein
folding, a chemical action that is directly linked to the maintenance of cell function through …
folding, a chemical action that is directly linked to the maintenance of cell function through …
Dissecting the thermodynamics of ATP binding to GroEL one nucleotide at a time
Variable-temperature electrospray ionization (vT-ESI) native mass spectrometry (nMS) is
used to determine the thermodynamics for stepwise binding of up to 14 ATP molecules to …
used to determine the thermodynamics for stepwise binding of up to 14 ATP molecules to …
Exploiting the antibacterial mechanism of phenazine substances from Lysobacter antibioticus 13-6 against Xanthomonas oryzae pv. oryzicola
Q Liu, J Yang, W Ahmed, X Wan, L Wei, G Ji - Journal of Microbiology, 2022 - Springer
Bacterial leaf streak caused by Xanthomonas oryzae pv. oryzicola (Xoc) is one of the most
destructive diseases affecting rice production worldwide. In this study, we extracted and …
destructive diseases affecting rice production worldwide. In this study, we extracted and …
Native Capillary Electrophoresis–Mass Spectrometry of Near 1 MDa Non‐Covalent GroEL/GroES/Substrate Protein Complexes
AL Marie, F Georgescauld, KR Johnson… - Advanced …, 2024 - Wiley Online Library
Protein complexes are essential for proteins' folding and biological function. Currently,
native analysis of large multimeric protein complexes remains challenging. Structural …
native analysis of large multimeric protein complexes remains challenging. Structural …
[HTML][HTML] Visualizing chaperonin function in situ by cryo-electron tomography
Chaperonins are large barrel-shaped complexes that mediate ATP-dependent protein
folding,–. The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein …
folding,–. The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein …
From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study
DG Liebermann, J Jungwirth, I Riven… - The Journal of …, 2023 - ACS Publications
The chaperonin GroEL is a multisubunit molecular machine that assists in protein folding in
the Escherichia coli cytosol. Past studies have shown that GroEL undergoes large allosteric …
the Escherichia coli cytosol. Past studies have shown that GroEL undergoes large allosteric …
[HTML][HTML] Structural and computational study of the GroEL–Prion protein complex
AA Mamchur, AV Moiseenko, IS Panina… - Biomedicines, 2021 - mdpi.com
The molecular chaperone GroEL is designed to promote protein folding and prevent
aggregation. However, the interaction between GroEL and the prion protein, PrPC, could …
aggregation. However, the interaction between GroEL and the prion protein, PrPC, could …
[HTML][HTML] Evaluation and Characterization of the Insecticidal Activity and Synergistic Effects of Different GroEL Proteins from Bacteria Associated with …
A Rivera-Ramírez, R Salgado-Morales… - Toxins, 2023 - mdpi.com
GroEL is a chaperonin that helps other proteins fold correctly. However, alternative activities,
such as acting as an insect toxin, have also been discovered. This work evaluates the …
such as acting as an insect toxin, have also been discovered. This work evaluates the …