Residue 134 determines the dimer-tetramer assembly of nucleoside diphosphate kinase from moderately halophilic bacteria

FEBS Letters

Volumn 582, Issue 7, 2008, Pages 1049-1054

  Tokunaga, Hiroko ^a   Ishibashi, Matsujiro ^a   Arisaka, Fumio ^b   Arai, Shigeki ^c   Kuroki, Ryota ^c   Arakawa, Tsutomu ^d   Tokunaga, Masao ^a  

^a KAGOSHIMA UNIVERSITY   (Japan)

^b Tokyo Institute of Technology ^*  (Japan)

^c JAPAN ATOMIC ENERGY AGENCY   (Japan)

^d ALLIANCE PROTEIN LABORATORIES   (United States)

Author keywords

Chimeric protein; Cross linking; Halophilic; Nucleoside diphosphate kinase; Subunit assembly

Indexed keywords

DIMER; NUCLEOSIDE DIPHOSPHATE KINASE; TETRAMER;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CROSS LINKING; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STRUCTURE; GENE MUTATION; HALOMONAS; HALOPHILIC BACTERIUM; MYXOCOCCUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; DIMERIZATION; HALOMONAS; MODELS, MOLECULAR; NUCLEOSIDE-DIPHOSPHATE KINASE; PROTEIN SUBUNITS; PSEUDOMONAS;

HALOMONAS; MYXOCOCCUS; PSEUDOMONAS;

EID: 40849123928     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.02.054     Document Type: Article

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