3N38

Ribonucleotide Reductase NrdF from Escherichia coli Soaked with Ferrous Ions

Summary for 3N38

• Entry DOI: 10.2210/pdb3n38/pdb
• Related: 3N37 3N39 3N3A 3N3B
• Descriptor: Ribonucleoside-diphosphate reductase 2 subunit beta, FE (II) ION (3 entities in total)
• Functional Keywords: ribonucleotide reductase, four-helix bundle, diferrous cluster, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 36586.76

Authors

Boal, A.K.,Cotruvo Jr., J.A.,Stubbe, J.,Rosenzweig, A.C. (deposition date: 2010-05-19, release date: 2010-08-18, Last modification date: 2023-09-06)

Primary citation

Boal, A.K.,Cotruvo, J.A.,Stubbe, J.,Rosenzweig, A.C.
Structural basis for activation of class Ib ribonucleotide reductase.
Science, 329:1526-1530, 2010

PubMed Abstract: The class Ib ribonucleotide reductase of Escherichia coli can initiate reduction of nucleotides to deoxynucleotides with either a Mn(III)2-tyrosyl radical (Y•) or a Fe(III)2-Y• cofactor in the NrdF subunit. Whereas Fe(III)2-Y• can self-assemble from Fe(II)2-NrdF and O2, activation of Mn(II)2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2. The crystal structures reported here of E. coli Mn(II)2-NrdF and Fe(II)2-NrdF reveal different coordination environments, suggesting distinct initial binding sites for the oxidants during cofactor activation. In the structures of Mn(II)2-NrdF in complex with reduced and oxidized NrdI, a continuous channel connects the NrdI flavin cofactor to the NrdF Mn(II)2 active site. Crystallographic detection of a putative peroxide in this channel supports the proposed mechanism of Mn(III)2-Y• cofactor assembly.

PubMed: 20688982
DOI: 10.1126/science.1190187

Experimental method

X-RAY DIFFRACTION (1.9 Å)