1syy | pdb_00001syy
Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis
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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 with FE and PB as ligands. Active as Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 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 Wed Nov 21 02:51:38 2007
