1syy
From Proteopedia
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 Sat May 3 09:17:45 2008
