Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 9, 2009, Pages 1344-1354

  Machida, Kodai ^a,b   Fujiwara, Ryoko ^a,b   Tanaka, Tatsuhide ^a,b   Sakane, Isao ^a,b   Hongo, Kunihiro ^a,b   Mizobata, Tomohiro ^a,b   Kawata, Yasushi ^a,b  

^a TOTTORI UNIVERSITY   (Japan)

^b TOTTORI UNIVERSITY   (Japan)

Author keywords

Chaperonin; GroEL; GroEL GroES complex formation; Hinge 2 site; Protein folding; Structure and function

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONIN; GLYCINE; GLYCINE 192; GLYCINE 374; GLYCINE 375; UNCLASSIFIED DRUG;

ARTICLE; ENCAPSULATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE;

ADENOSINE TRIPHOSPHATE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GROEL PROTEIN; GROES PROTEIN; MODELS, MOLECULAR; POINT MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 69249229765     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.12.003     Document Type: Article

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