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New page: left|200px<br /><applet load="1syy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1syy, resolution 1.70Å" /> '''Crystal structure of...
 
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[[Image:1syy.gif|left|200px]]<br /><applet load="1syy" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1syy.gif|left|200px]]<br /><applet load="1syy" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1syy, resolution 1.70&Aring;" />
caption="1syy, resolution 1.70&Aring;" />
'''Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis'''<br />
'''Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis'''<br />


==Overview==
==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.
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==
==About this Structure==
1SYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis] with FE and PB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SYY OCA].  
1SYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=PB:'>PB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYY OCA].  


==Reference==
==Reference==
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[[Category: diiron; oxygen activation; iron coupled radical; immune evasion]]
[[Category: diiron; oxygen activation; iron coupled radical; immune evasion]]


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