1syy | pdb_00001syy
Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis
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| 1syy, resolution 1.70Å | |||||||||||||
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| Ligands: | FE, PB | ||||||||||||
| Gene: | NRDB, CT828 (Chlamydia trachomatis) | ||||||||||||
| Activity: | Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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 Sun Mar 30 23:48:49 2008
