ArticleThe Journal of biological chemistry2014
Asp-52 in combination with Asp-398 plays a critical role in ATP hydrolysis of chaperonin GroEL.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1.Cell stress & chaperones · 2026Article
- Density Functional Theory Calculations to Investigate the Role Played by an Aspartate Dyad in Hsp60-Catalyzed ATP Hydrolysis.The journal of physical chemistry letters · 2025Article
- Pathogenic mutation impairs functional dynamics of Hsp60 in mono- and oligomeric states.Nature communications · 2025Article
- Physicochemical Properties of the Mammalian Molecular Chaperone HSP60.International journal of molecular sciences · 2018Article
- Pseudomonas aeruginosa GroEL Stimulates Production of PTX3 by Activating the NF-κB Pathway and Simultaneously Downregulating MicroRNA-9.Infection and immunity · 2017Article
- Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins.Biophysics and physicobiology · 2016Review
- Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein.The Journal of biological chemistry · 2015Article
- Synergistic effects of ATP and RNA binding to human DEAD-box protein DDX1.Nucleic acids research · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli chaperonin GroEL is a double-ring chaperone that assists protein folding with the aid of GroES and ATP. Asp-398 in GroEL is known as one of the critical residues on ATP hydrolysis because GroEL(D398A) mutant is deficient in ATP hydrolysis (<2% of the wild type) but not in ATP binding. In the archaeal Group II chaperonin, another aspartate residue, Asp-52 in the corresponding E. coli GroEL, in addition to Asp-398 is also important for ATP hydrolysis. We investigated the role of Asp-52 in GroEL and found that ATPase activity of GroEL(D52A) and GroEL(D52A/D398A) mutants was ∼ 20% and <0.01% of wild-type GroEL, respectively, indicating that Asp-52 in E. coli GroEL is also involved in the ATP hydrolysis. GroEL(D52A/D398A) formed a symmetric football-shaped GroEL-GroES complex in the presence of ATP, again confirming the importance of the symmetric complex during the GroEL ATPase cycle. Notably, the symmetric complex of GroEL(D52A/D398A) was extremely stable, with a half-time of ∼ 150 h (∼ 6 days), providing a good model to characterize the football-shaped complex.
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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.