The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2

Journal of Molecular Biology

Volumn 262, Issue 5, 1996, Pages 706-720

  Kauppi, Björn ^a   Nielsen, Bettina B ^b   Ramaswamy, S ^a   Larsen, Ingrid Kjøller ^b   Thelander, Margareta ^c   Thelander, Lars ^c   Eklund, Hans ^a  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c UMEÅ UNIVERSITY   (Sweden)

Author keywords

Crystal structure; Hydrophobic channel; Iron binding; Ribonucleotide reductase; Tyrosyl radical inactivation

Indexed keywords

DIMER; FERRIC ION; IRON; RIBONUCLEOTIDE REDUCTASE; SERINE; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ESCHERICHIA COLI; MAMMAL; MOUSE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; STEREOCHEMISTRY;

ESCHERICHIA COLI; EUKARYOTA; LETHRINIDAE; MAMMALIA;

EID: 0030580112     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0546     Document Type: Article

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