8BT4
Ribonucleotide Reductase class Ie R2 from Mesoplasma florum, radical-lost ground state
Summary for 8BT4
| Entry DOI | 10.2210/pdb8bt4/pdb |
| Descriptor | Ribonucleoside-diphosphate reductase, CALCIUM ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | ribonucleotide reductase r2 subunit, ferritin-like superfamily, dopa post-translational modification, oxidoreductase |
| Biological source | Mesoplasma florum L1 |
| Total number of polymer chains | 2 |
| Total formula weight | 80414.03 |
| Authors | |
| Primary citation | Lebrette, H.,Srinivas, V.,John, J.,Aurelius, O.,Kumar, R.,Lundin, D.,Brewster, A.S.,Bhowmick, A.,Sirohiwal, A.,Kim, I.S.,Gul, S.,Pham, C.,Sutherlin, K.D.,Simon, P.,Butryn, A.,Aller, P.,Orville, A.M.,Fuller, F.D.,Alonso-Mori, R.,Batyuk, A.,Sauter, N.K.,Yachandra, V.K.,Yano, J.,Kaila, V.R.I.,Sjoberg, B.M.,Kern, J.,Roos, K.,Hogbom, M. Structure of a ribonucleotide reductase R2 protein radical. Science, 382:109-113, 2023 Cited by PubMed Abstract: Aerobic ribonucleotide reductases (RNRs) initiate synthesis of DNA building blocks by generating a free radical within the R2 subunit; the radical is subsequently shuttled to the catalytic R1 subunit through proton-coupled electron transfer (PCET). We present a high-resolution room temperature structure of the class Ie R2 protein radical captured by x-ray free electron laser serial femtosecond crystallography. The structure reveals conformational reorganization to shield the radical and connect it to the translocation path, with structural changes propagating to the surface where the protein interacts with the catalytic R1 subunit. Restructuring of the hydrogen bond network, including a notably short O-O interaction of 2.41 angstroms, likely tunes and gates the radical during PCET. These structural results help explain radical handling and mobilization in RNR and have general implications for radical transfer in proteins. PubMed: 37797025DOI: 10.1126/science.adh8160 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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