Structural highlights
Function
[RIR2_CHLTR] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The radical site in chlamydial ribonucleotide reductase defines a new R2 subclass.,Hogbom M, Stenmark P, Voevodskaya N, McClarty G, Graslund A, Nordlund P Science. 2004 Jul 9;305(5681):245-8. PMID:15247479[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 2004 Jul 9;305(5681):245-8. PMID:15247479 doi:10.1126/science.1098419
