7b9q
The SERp optimized structure of Ribonucleotide reductase from Rhodobacter sphaeroidesThe SERp optimized structure of Ribonucleotide reductase from Rhodobacter sphaeroides
Structural highlights
FunctionQ3J3H6_CERS4 Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.[ARBA:ARBA00025437][RuleBase:RU364064] Publication Abstract from PubMedRibonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to the corresponding deoxyribonucleotides. The catalytic activity of most RNRs depends on the formation of a dimer of the catalytic subunits. The active site is located at the interface, and part of the substrate binding site and regulatory mechanisms work across the subunit in the dimer. In this study, we describe and characterize a novel domain responsible for forming the catalytic dimer in several class II RNRs. The 3D structure of the class II RNR from Rhodobacter sphaeroides reveals a so far undescribed alpha-helical domain in the dimer interface, which is embracing the other subunit. Genetic removal of this HUG domain leads to a severe reduction of activity paired with reduced dimerization capability. In comparison with other described RNRs, the enzyme with this domain is less dependent on the presence of nucleotides to act as allosteric effectors in the formation of dimers. The HUG domain appears to serve as an interlock to keep the dimer intact and functional even at low enzyme and/or effector concentrations. HUG Domain Is Responsible for Active Dimer Stabilization in an NrdJd Ribonucleotide Reductase.,Fietze T, Wilk P, Kabinger F, Anoosheh S, Hofer A, Lundin D, Feiler CG, Weiss MS, Loderer C Biochemistry. 2022 Aug 2;61(15):1633-1641. doi: 10.1021/acs.biochem.2c00173. Epub, 2022 Jul 20. PMID:35856337[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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