Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding.

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Title: Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding.
Authors: Bimai O; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden., Banerjee I; Section for Biochemistry and Structural Biology, Centre for Molecular Protein Science, Department of Chemistry, Lund University, Lund, Sweden., Rozman Grinberg I; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden., Huang P; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden., Hultgren L; Structural Proteomics, SciLifeLab, Lund University, Lund, Sweden., Ekström S; Structural Proteomics, SciLifeLab, Lund University, Lund, Sweden., Lundin D; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden., Sjöberg BM; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden., Logan DT; Section for Biochemistry and Structural Biology, Centre for Molecular Protein Science, Department of Chemistry, Lund University, Lund, Sweden.; Cryo-EM for Life Science, SciLifeLab, Lund University, Lund, Sweden.
Source: ELife [Elife] 2024 Jul 05; Vol. 12. Date of Electronic Publication: 2024 Jul 05.
Publication Type: Journal Article
Journal Info: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
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  Data: Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding.
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  Data: <searchLink fieldCode="AU" term="%22Bimai+O%22">Bimai O</searchLink>; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.<br /><searchLink fieldCode="AU" term="%22Banerjee+I%22">Banerjee I</searchLink>; Section for Biochemistry and Structural Biology, Centre for Molecular Protein Science, Department of Chemistry, Lund University, Lund, Sweden.<br /><searchLink fieldCode="AU" term="%22Rozman+Grinberg+I%22">Rozman Grinberg I</searchLink>; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.<br /><searchLink fieldCode="AU" term="%22Huang+P%22">Huang P</searchLink>; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.<br /><searchLink fieldCode="AU" term="%22Hultgren+L%22">Hultgren L</searchLink>; Structural Proteomics, SciLifeLab, Lund University, Lund, Sweden.<br /><searchLink fieldCode="AU" term="%22Ekström+S%22">Ekström S</searchLink>; Structural Proteomics, SciLifeLab, Lund University, Lund, Sweden.<br /><searchLink fieldCode="AU" term="%22Lundin+D%22">Lundin D</searchLink>; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.<br /><searchLink fieldCode="AU" term="%22Sjöberg+BM%22">Sjöberg BM</searchLink>; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.<br /><searchLink fieldCode="AU" term="%22Logan+DT%22">Logan DT</searchLink>; Section for Biochemistry and Structural Biology, Centre for Molecular Protein Science, Department of Chemistry, Lund University, Lund, Sweden.; Cryo-EM for Life Science, SciLifeLab, Lund University, Lund, Sweden.
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              Text: 2024 Jul 05
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