1SYY
Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis
Summary for 1SYY
| Entry DOI | 10.2210/pdb1syy/pdb |
| Descriptor | Ribonucleoside-diphosphate reductase beta chain, FE (III) ION, LEAD (II) ION, ... (4 entities in total) |
| Functional Keywords | diiron; oxygen activation; iron coupled radical; immune evasion, replication, oxidoreductase |
| Biological source | Chlamydia trachomatis |
| Total number of polymer chains | 1 |
| Total formula weight | 40882.21 |
| Authors | Hogbom, M.,Stenmark, P.,Voevodskaya, N.,McClarty, G.,Graslund, A.,Nordlund, P. (deposition date: 2004-04-02, release date: 2004-07-13, Last modification date: 2024-02-14) |
| Primary citation | Hogbom, M.,Stenmark, P.,Voevodskaya, N.,McClarty, G.,Graslund, A.,Nordlund, P. The radical site in chlamydial ribonucleotide reductase defines a new R2 subclass. Science, 305:245-248, 2004 Cited by PubMed Abstract: Ribonucleotide reductase (RNR) synthesizes the deoxyribonucleotides for DNA synthesis. The R2 protein of normal class I ribonucleotide reductases contains a diiron site that produces a stable tyrosyl free radical, essential for enzymatic activity. Structural and electron paramagnetic resonance studies of R2 from Chlamydia trachomatis reveal a protein lacking a tyrosyl radical site. Instead, the protein yields an iron-coupled radical upon reconstitution. The coordinating structure of the diiron site is similar to that of diiron oxidases/monoxygenases and supports a role for this radical in the RNR mechanism. The specific ligand pattern in the C. trachomatis R2 metal site characterizes a new group of R2 proteins that so far has been found in eight organisms, three of which are human pathogens. PubMed: 15247479DOI: 10.1126/science.1098419 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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