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Article

Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL.

The Journal of biological chemistry - 13 Jan 2006

Koike-Takeshita Ayumi, Shimamura Tatsuro, Yokoyama Ken, Yoshida Masasuke, Taguchi Hideki

Abstract excerpt

In the crystal structure of the native GroEL.GroES.substrate protein complex from Thermus thermophilus, one GroEL subunit makes contact with two GroES subunits. One contact is through the H-I helices, and the other is through a novel GXXLE region. The side chain of Leu, in the GXXLE region, forms a hydrophobic cluster with residues of the H helix (Shimamura, T., Koike-Takeshita, A., Yokoyama, K., Masui, R.,...

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Identifiers

PMID: 16239229
DOI: 10.1074/jbc.M506298200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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