The ten-stranded beta/alpha barrel in ribonucleotide reductase protein R1.
The large subunit of ribonucleotide reductase (RNR) contains a ten-stranded beta/alpha barrel of a new type consisting of two antiparallel halves. The two halves of the barrel are pseudo 2-fold-related, have similar folds but different additional intervening secondary structure elements and loops. The inner diameter of the RNR barrel, 15 A to 20 A, is significantly larger than for the (beta alpha)3 barrels. The larger barrel forms a stable framework which holds an inserted hairpin loop rigidly and exposes active site residues at its tip. The barrel organization allows three cysteine residues to be positioned close to each other without forming unfavorable disulfide bridges between Cys439 on the tip of the inserted loop and the redox-active cysteine residues on the barrel strands. Redox-active cysteine residues separated by more than 200 residues are held in close proximity to each other on adjacent barrel strands.
Uhlin
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Department of Molecular Biology, Swedish University of Agricultural Sciences Uppsala Biomedical Center, Sweden.
Eklund
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H
D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004735:Energy Transfer; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012264:Ribonucleotide Reductases / Q000737:chemistry* / Q000378:metabolism; D014305:Triose-Phosphate Isomerase / Q000737:chemistry / Q000378:metabolism
D012264:Ribonucleotide Reductases; D014305:Triose-Phosphate Isomerase