4U3E
Anaerobic ribonucleotide reductase
Summary for 4U3E
Entry DOI | 10.2210/pdb4u3e/pdb |
Descriptor | Ribonucleoside triphosphate reductase, ZINC ION, CITRIC ACID, ... (7 entities in total) |
Functional Keywords | proteolysis, barrel, reductase, radical, oxidoreductase |
Biological source | Thermotoga maritima |
Total number of polymer chains | 2 |
Total formula weight | 158442.46 |
Authors | Funk, M.A.,Drennan, C.L. (deposition date: 2014-07-20, release date: 2014-09-03, Last modification date: 2024-10-23) |
Primary citation | Wei, Y.,Funk, M.A.,Rosado, L.A.,Baek, J.,Drennan, C.L.,Stubbe, J. The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant. Proc.Natl.Acad.Sci.USA, 111:E3756-E3765, 2014 Cited by PubMed Abstract: 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. PubMed: 25157154DOI: 10.1073/pnas.1414396111 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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