A structural mechanism for dimeric to tetrameric oligomer conversion in Halomonas sp. nucleoside diphosphate kinase

Protein Science

Volumn 21, Issue 4, 2012, Pages 498-510

  Arai, Shigeki ^a   Yonezawa, Yasushi ^a   Okazaki, Nobuo ^a   Matsumoto, Fumiko ^a   Tamada, Taro ^a   Tokunaga, Hiroko ^b   Ishibashi, Matsujiro ^b   Blaber, Michael ^a,c   Tokunaga, Masao ^b   Kuroki, Ryota ^a  

^a JAPAN ATOMIC ENERGY AGENCY   (Japan)

^b KAGOSHIMA UNIVERSITY   (Japan)

^c FLORIDA STATE UNIVERSITY COLLEGE OF MEDICINE   (United States)

Author keywords

Halophilic enzyme; Light scattering; Nucleoside diphosphate kinase; Oligomerization; X ray crystallography

Indexed keywords

CARBON; DIMER; NUCLEOSIDE DIPHOSPHATE KINASE; OLIGOMER; TETRAMER;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME SUBSTRATE; HALOMONAS; LIGHT SCATTERING; MOLECULAR WEIGHT; MUTANT; MUTATION; MYXOCOCCUS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; THERMOSTABILITY; WILD TYPE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CATALYTIC DOMAIN; CHROMATOGRAPHY, GEL; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ENZYME ASSAYS; ESCHERICHIA COLI; HALOMONAS; HYDROGEN BONDING; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; NUCLEOSIDE-DIPHOSPHATE KINASE; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; SEQUENCE ALIGNMENT; STATIC ELECTRICITY; SUBSTRATE SPECIFICITY;

HALOMONAS; HALOMONAS SP. #593; MYXOCOCCUS;

EID: 84858686534     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2032     Document Type: Article

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