3UUS
Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex
Summary for 3UUS
| Entry DOI | 10.2210/pdb3uus/pdb |
| Descriptor | Ribonucleoside-diphosphate reductase 1 subunit alpha, Ribonucleoside-diphosphate reductase 1 subunit beta, 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | 10 stranded alpha/beta barrel, datp bound, di-iron, oxidoreductase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 8 |
| Total formula weight | 521592.01 |
| Authors | Zimanyi, C.M.,Drennan, C.L. (deposition date: 2011-11-28, release date: 2011-12-21, Last modification date: 2024-11-20) |
| Primary citation | Ando, N.,Brignole, E.J.,Zimanyi, C.M.,Funk, M.A.,Yokoyama, K.,Asturias, F.J.,Stubbe, J.,Drennan, C.L. Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase. Proc.Natl.Acad.Sci.USA, 108:21046-21051, 2011 Cited by PubMed Abstract: Essential for DNA biosynthesis and repair, ribonucleotide reductases (RNRs) convert ribonucleotides to deoxyribonucleotides via radical-based chemistry. Although long known that allosteric regulation of RNR activity is vital for cell health, the molecular basis of this regulation has been enigmatic, largely due to a lack of structural information about how the catalytic subunit (α(2)) and the radical-generation subunit (β(2)) interact. Here we present the first structure of a complex between α(2) and β(2) subunits for the prototypic RNR from Escherichia coli. Using four techniques (small-angle X-ray scattering, X-ray crystallography, electron microscopy, and analytical ultracentrifugation), we describe an unprecedented α(4)β(4) ring-like structure in the presence of the negative activity effector dATP and provide structural support for an active α(2)β(2) configuration. We demonstrate that, under physiological conditions, E. coli RNR exists as a mixture of transient α(2)β(2) and α(4)β(4) species whose distributions are modulated by allosteric effectors. We further show that this interconversion between α(2)β(2) and α(4)β(4) entails dramatic subunit rearrangements, providing a stunning molecular explanation for the allosteric regulation of RNR activity in E. coli. PubMed: 22160671DOI: 10.1073/pnas.1112715108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (5.65 Å) |
Structure validation
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