Structure of the large subunit of class Ib ribonucleotide reductase from Salmonella typhimurium and its complexes with allosteric effectors

Journal of Molecular Biology

Volumn 330, Issue 1, 2003, Pages 87-97

  Uppsten, Malin ^a   Färnegårdh, Mathias ^a,d   Jordan, Albert ^b   Eliasson, Rolf ^c,e   Eklund, Hans ^a   Uhlin, Ulla ^a  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^c KAROLINSKA INSTITUTE   (Sweden)

^d Karo Bio   (Sweden)

^e STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

Active site cysteine residues; Allosteric effectors; Catalytic subunit; Ribonucleotide reductase

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYSTEINE; DISULFIDE; NUCLEOTIDE; PROTEIN SUBUNIT; RIBONUCLEOTIDE REDUCTASE; THIOL DERIVATIVE; TYROSINE; 2'-DEOXYADENOSINE TRIPHOSPHATE; 2'-DEOXYCYTIDINE 5'-TRIPHOSPHATE; DEOXYADENOSINE PHOSPHATE; DEOXYADENOSINE TRIPHOSPHATE; DEOXYCYTIDINE PHOSPHATE; DEOXYCYTIDINE TRIPHOSPHATE; PYRIMIDINE NUCLEOTIDE; RIBONUCLEOTIDE REDUCTASE R2 SUBUNIT; THYMIDINE 5'-TRIPHOSPHATE; THYMIDINE TRIPHOSPHATE;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; DIMERIZATION; ENZYMOLOGY; MACROMOLECULE; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI; SALMONELLA TYPHIMURIUM;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DEOXYADENINE NUCLEOTIDES; DEOXYCYTOSINE NUCLEOTIDES; DIMERIZATION; ESCHERICHIA COLI; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN SUBUNITS; RIBONUCLEOTIDE REDUCTASES; SALMONELLA TYPHIMURIUM; SEQUENCE HOMOLOGY, AMINO ACID; THYMINE NUCLEOTIDES;

EID: 0038342690     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00538-2     Document Type: Article

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