The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer

Nature Structural Biology

Volumn 9, Issue 4, 2002, Pages 293-300

  Sintchak, Michael D ^a   Arjara, Gitrada ^a   Kellogg, Brenda A ^a   Stubbe, JoAnne ^a   Drennan, Catherine L ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE DERIVATIVE; ADENINYLPENTYLCOBALAMIN; DEOXYRIBONUCLEOTIDE; RIBONUCLEOSIDE TRIPHOSPHATE REDUCTASE; RIBONUCLEOTIDE; RIBONUCLEOTIDE REDUCTASE; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DNA REPAIR; DNA REPLICATION; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; LACTOBACILLUS; LACTOBACILLUS LEICHMANNII; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE;

ALLOSTERIC REGULATION; APOENZYMES; BINDING SITES; CATALYSIS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; EVOLUTION, MOLECULAR; FREE RADICALS; LACTOBACILLUS; MODELS, MOLECULAR; ORGANOMETALLIC COMPOUNDS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RIBONUCLEOTIDE REDUCTASES; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; SULFUR;

INSERTION SEQUENCES; LACTOBACILLUS; LACTOBACILLUS LEICHMANNII;

EID: 0036219377     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb774     Document Type: Article

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