4u3e

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u3e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u3e RCSB], [http://www.ebi.ac.uk/pdbsum/4u3e PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u3e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u3e RCSB], [http://www.ebi.ac.uk/pdbsum/4u3e PDBsum]</span></td></tr>
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== Publication Abstract from PubMed ==
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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.
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The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant.,Wei Y, Funk MA, Rosado LA, Baek J, Drennan CL, Stubbe J Proc Natl Acad Sci U S A. 2014 Sep 9;111(36):E3756-65. doi:, 10.1073/pnas.1414396111. Epub 2014 Aug 25. PMID:25157154<ref>PMID:25157154</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 21:48, 1 October 2014

Anaerobic ribonucleotide reductase

4u3e, resolution 1.64Å

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