GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps

Journal of Biological Chemistry

Volumn 271, Issue 45, 1996, Pages 28229-28234

  Murai, Noriyuki ^a   Makino, Yoshihide ^a   Yoshida, Masasuke ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ASPARTIC ACID; CHAPERONIN; CYSTEINE; DITHIOTHREITOL; MALATE DEHYDROGENASE; POLYPEPTIDE; SERINE;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; NONHUMAN; OXIDATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN FOLDING;

3-ISOPROPYLMALATE DEHYDROGENASE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ALCOHOL OXIDOREDUCTASES; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DITHIOTHREITOL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GROEL PROTEIN; GROES PROTEIN; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PEPTIDES; PROTEIN CONFORMATION;

EID: 0029903725     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.45.28229     Document Type: Article

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