Volume 2, Issue 9, Pages 793-796 (September 1994) The ribonucleotide reductase jigsaw puzzle: a large piece falls into place  Britt-Marie Sjöberg  Structure  Volume 2, Issue 9, Pages 793-796 (September 1994) DOI: 10.1016/S0969-2126(94)00080-8

Figure 1 Proposed reaction mechanism for biosynthesis of deoxyribonucleotides. See text for details. Structure 1994 2, 793-796DOI: (10.1016/S0969-2126(94)00080-8)

Figure 2 The R1 structure. (a) The 10-stranded α/β barrel with the three active site cysteines highlighted. The first half of the barrel is yellow, the second half green and the connecting strand is magenta. (b) Three-dimensional structure of the R1 dimer. The amino terminal domain is blue, the α/β barrel is yellow with the β-strands in orange. The small domain shown in gray covers the bottom of the barrel. The synthetic R2 peptide, which was found to be necessary for good crystallization, is shown in red. Figures reproduced from [7], with permission. Structure 1994 2, 793-796DOI: (10.1016/S0969-2126(94)00080-8)

Figure 3 Proposed electron transfer pathway within E. coli ribonucleotide reductase shown with a model-built substrate nucleotide in the active site. Residues from the R2 protein are labeled in red, those from R1 are labeled in yellow. Fe1 is hown as a pink sphere, and the proposed path is shown as a white dotted line. Structure 1994 2, 793-796DOI: (10.1016/S0969-2126(94)00080-8)