Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH

Journal of Biological Chemistry

Volumn 274, Issue 37, 1999, Pages 26225-26232

  Karata, Kiyonobu ^a   Inagawa, Takabumi ^a   Wilkinson, Anthony J ^b   Tatsuta, Takashi ^a   Ogura, Teru ^a  

^a KUMAMOTO UNIV SCHOOL OF MEDICINE   (Japan)

^b UNIVERSITY OF YORK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; HYBRID PROTEIN; MUTANT PROTEIN; PROTEINASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME MECHANISM; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; SEQUENCE HOMOLOGY;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ATP-DEPENDENT PROTEASES; BACTERIAL PROTEINS; CONSERVED SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033543650     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.37.26225     Document Type: Article

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