Crystal structure of Escherichia coli MazG, the regulator of nutritional stress response

Journal of Biological Chemistry

Volumn 283, Issue 22, 2008, Pages 15232-15240

  Lee, Sujin ^a   Myung, Hee Kim ^b   Beom, Sik Kang ^c   Kim, Jeong Sun ^d   Kim, Ghyung Hwa ^a   Kim, Yeon Gil ^a   Kyung, Jin Kim ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

^b Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^c Kyungpook National University   (South Korea)

^d Chonnam National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMINO ACIDS; CELL DEATH; ESCHERICHIA COLI; ORGANIC ACIDS;

ACTIVE SITES; BACTERIAL CELLS; C TERMINUSES; CATALYTIC DOMAINS; CELL SURVIVALS; CELLULAR LEVELS; COMPLEX STRUCTURES; E. COLI; ENZYMATIC ACTIVITIES; GLOBULAR DOMAINS; GUANOSINE; IN VITRO; IN-VIVO; MUTAGENESIS STUDIES; NUCLEOSIDE TRIPHOSPHATE; NUCLEOSIDE TRIPHOSPHATES; NUTRIENT STARVATIONS; NUTRITIONAL STRESSES; PROGRAMMED CELL DEATHS; TERMINAL DOMAINS;

CRYSTAL STRUCTURE;

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; BACTERIAL ENZYME MAZG; HYDROLASE; HYDROLASE NTPASE; INORGANIC PYROPHOSPHATASE; NUCLEOSIDE TRIPHOSPHATE; UNCLASSIFIED DRUG; DRUG DERIVATIVE; ESCHERICHIA COLI PROTEIN; GUANOSINE; NUCLEOSIDE TRIPHOSPHATASE; NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHATASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; MUTAGENESIS; NUTRITION; PRIORITY JOURNAL; PROTEIN FOLDING; STRESS; BACTERIAL CHROMOSOME; BINDING SITE; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; PHYSIOLOGY; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

BINDING SITES; CATALYTIC DOMAIN; CHROMOSOMES, BACTERIAL; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GUANOSINE; MUTAGENESIS; NUCLEOSIDE-TRIPHOSPHATASE; PROTEIN FOLDING; PYROPHOSPHATASES;

EID: 47249083116     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M800479200     Document Type: Article

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