Asp-52 in combination with Asp-398 plays a critical role in ATP hydrolysis of chaperonin GroEL

Journal of Biological Chemistry

Volumn 289, Issue 43, 2014, Pages 30005-30011

  Koike Takeshita, Ayumi ^a   Mitsuoka, Kaoru ^b   Taguchi, Hideki ^c  

^a KANAGAWA INSTITUTE OF TECHNOLOGY   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^c TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; SPORTS;

ARCHAEAL; ASPARTATE RESIDUE; ATP BINDING; ATP HYDROLYSIS; ATP-ASE ACTIVITY; CHAPERONIN; SYMMETRIC COMPLEXES; WILD TYPES;

HYDROLYSIS;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE; ASPARTIC ACID; CHAPERONIN 60; EARLY PREGNANCY FACTOR; MUTANT PROTEIN; MALATE DEHYDROGENASE; PROTEIN SUBUNIT; THIOSULFATE SULFURTRANSFERASE;

ARTICLE; COMPLEX FORMATION; ESCHERICHIA COLI; NONHUMAN; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; WILD TYPE; BINDING SITE; CHEMISTRY; HYDROLYSIS; METABOLISM; PROTEIN FOLDING; PROTEIN SUBUNIT; STAINING; STRUCTURE ACTIVITY RELATION; ULTRASTRUCTURE;

ADENOSINE TRIPHOSPHATE; ASPARTIC ACID; BINDING SITES; CHAPERONIN 10; CHAPERONIN 60; ESCHERICHIA COLI; HYDROLYSIS; MALATE DEHYDROGENASE; MUTANT PROTEINS; NEGATIVE STAINING; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN SUBUNITS; STRUCTURE-ACTIVITY RELATIONSHIP; THIOSULFATE SULFURTRANSFERASE;

EID: 84907826095     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.593822     Document Type: Article

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