My NCBI | Sign In
RSS Settings
  • Search:

Display Settings:

Format

Send to:

Choose Destination

    Structure. 2004 Aug;12(8):1471-80.

    Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.

    Shimamura T, Koike-Takeshita A, Yokoyama K, Masui R, Murai N, Yoshida M, Taguchi H, Iwata S.

    Department of Biological Sciences, Imperial College London, London SW7 2AZ, United Kingdom.

    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.

    PMID: 15296740 [PubMed - indexed for MEDLINE]

    Publication Types, MeSH Terms, Substances, Secondary Source ID

    Publication Types:

    MeSH Terms:

    Substances:

    Secondary Source ID:

    LinkOut - more resources

    Full Text Sources:

    Supplemental Content

    Click here to read

    Related articles

    Cited by 5 PubMed Central articles

    Structures reported by this article

    All links from this record

    • Related Articles

      Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.

    • Gene

      Gene records that cite the current articles. Citations in Gene are added manually by NCBI or imported from outside public resources.

    • Nucleotide (Weighted)

      Nucleotide records associated with the current articles through the Gene database. These are the related sequences on the Gene record that are added manually by NCBI.

    • Protein (RefSeq)

      NCBI protein Reference Sequences (RefSeqs) that are cited in the current articles, included in the corresponding Gene Reference into Function, or that include the PubMed articles as references.

    • Protein (Weighted)

      Protein records associated with the current articles through related Gene database records. These are the related sequences on the Gene record that are added manually by NCBI.

    • Protein Clusters

      Clusters of related proteins from the Protein Clusters database that cite the current articles. Sources of references in Protein Clusters include the associated Gene and Conserved Domain records as well as NCBI added citations.

    • Taxonomy via GenBank

      Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).

    • Protein

      Protein translation features of primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.

    • Structure

      Three-dimensional structure records in the NCBI Structure database for data reported in the current articles.

    • 3D Domains

      Structural domains in the NCBI Structure database that are parts of the 3D structures reported in the current articles.

    • Cited in PMC

      Full-text articles in the PubMed Central Database that cite the current articles.

    Recent activity