8P2S
| Cryo-EM structure of the anaerobic ribonucleotide reductase from Prevotella copri in its dimeric, ATP/dTTP/GTP-bound state | Descriptor: | Anaerobic ribonucleoside-triphosphate reductase, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... | Authors: | Bimai, O, Banerjee, I, Sjoberg, B.M, Logan, D.T. | Deposit date: | 2023-05-16 | Release date: | 2023-09-13 | Last modified: | 2024-09-25 | Method: | ELECTRON MICROSCOPY (2.4 Å) | Cite: | Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding. Elife, 12, 2024
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8P39
| Cryo-EM structure of the anaerobic ribonucleotide reductase from Prevotella copri in its dimeric, dGTP/ATP-bound state | Descriptor: | 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, Anaerobic ribonucleoside-triphosphate reductase, ... | Authors: | Bimai, O, Banerjee, I, Sjoberg, B.M, Logan, D.T. | Deposit date: | 2023-05-17 | Release date: | 2023-09-13 | Last modified: | 2024-09-25 | Method: | ELECTRON MICROSCOPY (2.58 Å) | Cite: | Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding. Elife, 12, 2024
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8P2C
| Cryo-EM structure of the anaerobic ribonucleotide reductase from Prevotella copri in its tetrameric state produced in the presence of dATP and CTP | Descriptor: | 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE, Anaerobic ribonucleoside-triphosphate reductase, MAGNESIUM ION | Authors: | Banerjee, I, Bimai, O, Sjoberg, B.M, Logan, D.T. | Deposit date: | 2023-05-15 | Release date: | 2023-09-13 | Last modified: | 2024-09-25 | Method: | ELECTRON MICROSCOPY (2.59 Å) | Cite: | Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding. Elife, 12, 2024
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8P2D
| Cryo-EM structure of the dimeric form of the anaerobic ribonucleotide reductase from Prevotella copri produced in the presence of dATP and CTP | Descriptor: | 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE, Anaerobic ribonucleoside-triphosphate reductase, MAGNESIUM ION | Authors: | Banerjee, I, Bimai, O, Sjoberg, B.M, Logan, D.T. | Deposit date: | 2023-05-15 | Release date: | 2023-09-13 | Last modified: | 2024-09-25 | Method: | ELECTRON MICROSCOPY (2.59 Å) | Cite: | Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding. Elife, 12, 2024
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8P27
| Cryo-EM structure of the anaerobic ribonucleotide reductase from Prevotella copri in its dimeric, dATP-bound state | Descriptor: | 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE, Anaerobic ribonucleoside-triphosphate reductase, MAGNESIUM ION | Authors: | Banerjee, I, Bimai, O, Sjoberg, B.M, Logan, D.T. | Deposit date: | 2023-05-15 | Release date: | 2023-08-30 | Last modified: | 2024-09-25 | Method: | ELECTRON MICROSCOPY (2.73 Å) | Cite: | Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding. Elife, 12, 2024
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8P28
| Cryo-EM structure of the anaerobic ribonucleotide reductase from Prevotella copri in its tetrameric, dATP-bound state | Descriptor: | 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE, Anaerobic ribonucleoside-triphosphate reductase, MAGNESIUM ION | Authors: | Banerjee, I, Bimai, O, Sjoberg, B.M, Logan, D.T. | Deposit date: | 2023-05-15 | Release date: | 2023-08-30 | Last modified: | 2024-09-25 | Method: | ELECTRON MICROSCOPY (2.77 Å) | Cite: | Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding. Elife, 12, 2024
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8P23
| Cryo-EM structure of the anaerobic ribonucleotide reductase from Prevotella copri in its dimeric, ATP/CTP-bound state | Descriptor: | ADENOSINE-5'-TRIPHOSPHATE, Anaerobic ribonucleoside-triphosphate reductase, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Banerjee, I, Bimai, O, Sjoberg, B.M, Logan, D.T. | Deposit date: | 2023-05-14 | Release date: | 2023-08-30 | Last modified: | 2024-09-25 | Method: | ELECTRON MICROSCOPY (3.17 Å) | Cite: | Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding. Elife, 12, 2024
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