Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8 Å reveals rearrangement between two GroEL rings

Journal of Molecular Biology

Volumn 426, Issue 21, 2014, Pages 3634-3641

  Koike Takeshita, Ayumi ^a   Arakawa, Takatoshi ^b   Taguchi, Hideki ^c   Shimamura, Tatsuro ^b,d  

^a KANAGAWA INSTITUTE OF TECHNOLOGY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^d JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

chaperone; chaperonin; folding; inter ring contacts; nanomachine

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE 14; CHAPERONIN; CHAPERONIN GROEL; GROES2 PROTEIN; UNCLASSIFIED DRUG; CHAPERONIN 60; EARLY PREGNANCY FACTOR; PROTEIN BINDING;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLIZATION; ESCHERICHIA COLI; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DETERMINATION; PROTEIN FOLDING; PROTEIN HYDROLYSIS; PROTEIN STRUCTURE; REACTION ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; HYDROLYSIS; MUTATION; NANOTECHNOLOGY; PROCEDURES; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATE; CHAPERONIN 10; CHAPERONIN 60; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDROLYSIS; MODELS, MOLECULAR; MUTATION; NANOTECHNOLOGY; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

EID: 84907822084     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.08.017     Document Type: Article

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