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HUG Domain Is Respo...
HUG Domain Is Responsible for Active Dimer Stabilization in an NrdJd Ribonucleotide Reductase
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- Fietze, Tobias (author)
- Chair of Molecular Biotechnology, Technische Universität Dresden, Dresden, Germany
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- Wilk, Piotr (author)
- Macromolecular Crystallography, Helmholtz-Zentrum Berlin, Berlin, Germany; Malopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow, Poland
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- Kabinger, Florian (author)
- Department of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany
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- Anoosheh, Saber (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Hofer, Anders (author)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Lundin, Daniel, 1965- (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden
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- Feiler, Christian G. (author)
- Macromolecular Crystallography, Helmholtz-Zentrum Berlin, Berlin, Germany
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- Weiss, Manfred S. (author)
- Macromolecular Crystallography, Helmholtz-Zentrum Berlin, Berlin, Germany
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- Loderer, Christoph (author)
- Chair of Molecular Biotechnology, Technische Universität Dresden, Dresden, Germany
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(creator_code:org_t)
- 2022-07-20
- 2022
- English.
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In: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 61:15, s. 1633-1641
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- Ribonucleotide 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 α-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.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Fietze, Tobias
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Wilk, Piotr
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Kabinger, Floria ...
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Anoosheh, Saber
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Hofer, Anders
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Lundin, Daniel, ...
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show more...
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Feiler, Christia ...
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Weiss, Manfred S ...
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Loderer, Christo ...
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
- Articles in the publication
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Biochemistry
- By the university
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Stockholm University
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Umeå University