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Crystal structure of wild-type chaperonin GroEL.

Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H
J Mol Biol 354 940-51 (2005)
Cited: 56 times
EuropePMC logo PMID: 16288915

Abstract

The 2.9A resolution crystal structure of apo wild-type GroEL was determined for the first time and represents the reference structure, facilitating the study of structural and functional differences observed in GroEL variants. Until now the crystal structure of the mutant Arg13Gly, Ala126Val GroEL was used for this purpose. We show that, due to the mutations as well as to the presence of a crystallographic symmetry, the ring-ring interface was inaccurately described. Analysis of the present structure allowed the definition of structural elements at this interface, essential for understanding the inter-ring allosteric signal transmission. We also show unambiguously that there is no ATP-induced 102 degrees rotation of the apical domain helix I around its helical axis, as previously assumed in the crystal structure of the (GroEL-KMgATP)(14) complex, and analyze the apical domain movements. These results enabled us to compare our structure with other GroEL crystal structures already published, allowing us to suggest a new route through which the allosteric signal for negative cooperativity propagates within the molecule. The proposed mechanism, supported by known mutagenesis data, underlines the importance of the switching of salt bridges.

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  20. Probing the Interaction of Huntingtin Exon-1 Polypeptides with the Chaperonin Nanomachine GroEL. Wälti MA, Kotler SA, Clore GM. Chembiochem 22 1985-1991 (2021)
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Reviews citing this publication (7)

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  2. Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases. Thomsen ND, Berger JM. Mol Microbiol 69 1071-1090 (2008)
  3. Dynamics, flexibility, and allostery in molecular chaperonins. Skjærven L, Cuellar J, Martinez A, Valpuesta JM. FEBS Lett 589 2522-2532 (2015)
  4. The complexity of chloroplast chaperonins. Vitlin Gruber A, Nisemblat S, Azem A, Weiss C. Trends Plant Sci 18 688-694 (2013)
  5. Dynamic Complexes in the Chaperonin-Mediated Protein Folding Cycle. Weiss C, Jebara F, Nisemblat S, Azem A. Front Mol Biosci 3 80 (2016)
  6. Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins. Iizuka R, Funatsu T. Biophys Physicobiol 13 63-69 (2016)
  7. Cryo-EM Analyses Permit Visualization of Structural Polymorphism of Biological Macromolecules. Chang WH, Huang SH, Lin HH, Chung SC, Tu IP. Front Bioinform 1 788308 (2021)

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  1. Large-scale conformational sampling of proteins using temperature-accelerated molecular dynamics. Abrams CF, Vanden-Eijnden E. Proc Natl Acad Sci U S A 107 4961-4966 (2010)
  2. Single particle analysis based on Zernike phase contrast transmission electron microscopy. Danev R, Nagayama K. J Struct Biol 161 211-218 (2008)
  3. Principal component and normal mode analysis of proteins; a quantitative comparison using the GroEL subunit. Skjaerven L, Martinez A, Reuter N. Proteins 79 232-243 (2011)
  4. Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis. Danziger O, Shimon L, Horovitz A. Protein Sci 15 1270-1276 (2006)
  5. Probing dynamics and conformational change of the GroEL-GroES complex by 13C NMR spectroscopy. Nishida N, Motojima F, Idota M, Fujikawa H, Yoshida M, Shimada I, Kato K. J Biochem 140 591-598 (2006)
  6. Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin. Sielaff B, Lee KS, Tsai FT. J Mol Biol 405 831-839 (2011)
  7. The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20. Vitlin Gruber A, Zizelski G, Azem A, Weiss C. PLoS One 9 e113835 (2014)
  8. Chaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomer. Pilak O, Harrop SJ, Siddiqui KS, Chong K, De Francisci D, Burg D, Williams TJ, Cavicchioli R, Curmi PM. Environ Microbiol 13 2232-2249 (2011)
  9. Temperature Regulates Stability, Ligand Binding (Mg2+ and ATP), and Stoichiometry of GroEL-GroES Complexes. Walker TE, Shirzadeh M, Sun HM, McCabe JW, Roth A, Moghadamchargari Z, Clemmer DE, Laganowsky A, Rye H, Russell DH. J Am Chem Soc 144 2667-2678 (2022)
  10. GroEL2 of Mycobacterium tuberculosis Reveals the Importance of Structural Pliability in Chaperonin Function. Chilukoti N, Kumar CM, Mande SC. J Bacteriol 198 486-497 (2016)
  11. A dynamic model of long-range conformational adaptations triggered by nucleotide binding in GroEL-GroES. Skjaerven L, Muga A, Reuter N, Martinez A. Proteins 80 2333-2346 (2012)
  12. Evaluation and Characterization of the Insecticidal Activity and Synergistic Effects of Different GroEL Proteins from Bacteria Associated with Entomopathogenic Nematodes on Galleria mellonella. Rivera-Ramírez A, Salgado-Morales R, Onofre-Lemus J, García-Gómez BI, Lanz-Mendoza H, Dantán-González E. Toxins (Basel) 15 623 (2023)
  13. Local Flexibility of a New Single-Ring Chaperonin Encoded by Bacteriophage AR9 Bacillus subtilis. Sokolova OS, Pichkur EB, Maslova ES, Kurochkina LP, Semenyuk PI, Konarev PV, Samygina VR, Stanishneva-Konovalova TB. Biomedicines 10 2347 (2022)
  14. Novel convergence-oriented approach for evaluation and optimization of workflow in single-particle two-dimensional averaging of electron microscope images. Moriya T, Mio K, Sato C. Microscopy (Oxf) 62 491-513 (2013)


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