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Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.
Structure. 2004 Aug; 12(8):1471-80.S

Abstract

The chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein, ATP, and GroES, generating a ternary complex in which protein folding occurs within the cavity capped by GroES (cis-cavity). We determined the crystal structure of the native GroEL-GroES-ADP homolog from Thermus thermophilus, with substrate proteins in the cis-cavity, at 2.8 A resolution. Twenty-four in vivo substrate proteins within the cis-cavity were identified from the crystals. The structure around the cis-cavity, which encapsulates substrate proteins, shows significant differences from that observed for the substrate-free Escherichia coli GroEL-GroES complex. The apical domain around the cis-cavity of the Thermus GroEL-GroES complex exhibits a large deviation from the 7-fold symmetry. As a result, the GroEL-GroES interface differs considerably from the previously reported E. coli GroEL-GroES complex, including a previously unknown contact between GroEL and GroES.

Authors+Show Affiliations

Shimamura T
Department of Biological Sciences, Imperial College London, London SW7 2AZ, United Kingdom.
Koike-Takeshita A
No affiliation info available
Yokoyama K
No affiliation info available
Masui R
No affiliation info available
Murai N
No affiliation info available
Yoshida M
No affiliation info available
Taguchi H
No affiliation info available
Iwata S
No affiliation info available

MeSH

Amino Acid SequenceChaperonin 10Chaperonin 60Crystallography, X-RayEscherichia coliMacromolecular SubstancesModels, MolecularMolecular Sequence DataSequence Homology, Amino AcidThermus thermophilus

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15296740

Citation

Shimamura, Tatsuro, et al. "Crystal Structure of the Native Chaperonin Complex From Thermus Thermophilus Revealed Unexpected Asymmetry at the Cis-cavity." Structure (London, England : 1993), vol. 12, no. 8, 2004, pp. 1471-80.
Shimamura T, Koike-Takeshita A, Yokoyama K, et al. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Structure. 2004;12(8):1471-80.
Shimamura, T., Koike-Takeshita, A., Yokoyama, K., Masui, R., Murai, N., Yoshida, M., Taguchi, H., & Iwata, S. (2004). Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Structure (London, England : 1993), 12(8), 1471-80.
Shimamura T, et al. Crystal Structure of the Native Chaperonin Complex From Thermus Thermophilus Revealed Unexpected Asymmetry at the Cis-cavity. Structure. 2004;12(8):1471-80. PubMed PMID: 15296740.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. AU - Shimamura,Tatsuro, AU - Koike-Takeshita,Ayumi, AU - Yokoyama,Ken, AU - Masui,Ryoji, AU - Murai,Noriyuki, AU - Yoshida,Masasuke, AU - Taguchi,Hideki, AU - Iwata,So, PY - 2004/02/27/received PY - 2004/05/05/revised PY - 2004/05/18/accepted PY - 2004/8/7/pubmed PY - 2005/1/20/medline PY - 2004/8/7/entrez SP - 1471 EP - 80 JF - Structure (London, England : 1993) JO - Structure VL - 12 IS - 8 N2 - The chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein, ATP, and GroES, generating a ternary complex in which protein folding occurs within the cavity capped by GroES (cis-cavity). We determined the crystal structure of the native GroEL-GroES-ADP homolog from Thermus thermophilus, with substrate proteins in the cis-cavity, at 2.8 A resolution. Twenty-four in vivo substrate proteins within the cis-cavity were identified from the crystals. The structure around the cis-cavity, which encapsulates substrate proteins, shows significant differences from that observed for the substrate-free Escherichia coli GroEL-GroES complex. The apical domain around the cis-cavity of the Thermus GroEL-GroES complex exhibits a large deviation from the 7-fold symmetry. As a result, the GroEL-GroES interface differs considerably from the previously reported E. coli GroEL-GroES complex, including a previously unknown contact between GroEL and GroES. SN - 0969-2126 UR - https://www.unboundmedicine.com/medline/citation/15296740/Crystal_structure_of_the_native_chaperonin_complex_from_Thermus_thermophilus_revealed_unexpected_asymmetry_at_the_cis_cavity_ DB - PRIME DP - Unbound Medicine ER -