The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant.

Publication Type:

Journal Article

Authors:

Wei, Yifeng; Funk, Michael A; Rosado, Leonardo A; Baek, Jiyeon; Drennan, Catherine L; Stubbe, JoAnne

Source:

Proc Natl Acad Sci U S A, Volume 111, Issue 36, p.E3756-65 (2014)

Keywords:

Amino Acids, Biocatalysis, Catalytic Domain, Computational Biology, Crystallography, X-Ray, Cytidine Triphosphate, Cytosine, Disulfides, Electron Spin Resonance Spectroscopy, Models, Biological, NADP, Neisseria, Oxidation-Reduction, Reducing Agents, Ribonucleotide Reductases, Thermotoga maritima, Thioredoxins, Time Factors

Abstract:

<p>The class III anaerobic ribonucleotide reductases (RNRs) studied to date couple the reduction of ribonucleotides to deoxynucleotides with the oxidation of formate to CO2. Here we report the cloning and heterologous expression of the Neisseria bacilliformis class III RNR and show that it can catalyze nucleotide reduction using the ubiquitous thioredoxin/thioredoxin reductase/NADPH system. We present a structural model based on a crystal structure of the homologous Thermotoga maritima class III RNR, showing its architecture and the position of conserved residues in the active site. Phylogenetic studies suggest that this form of class III RNR is present in bacteria and archaea that carry out diverse types of anaerobic metabolism.</p>

PDB: 
4U3E
Detector: 
Q315
Beamline: 
24-ID-C