1syy
From Proteopedia
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | NRDB, CT828 (Chlamydia trachomatis) | ||||||
| Activity: | Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis
Overview
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.
About this Structure
1SYY is a Single protein structure of sequence from Chlamydia trachomatis. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 14:11:26 2008
