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1syy
From Proteopedia
(New page: 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=" | + | [[Image:1syy.gif|left|200px]]<br /><applet load="1syy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1syy, resolution 1.70Å" /> | caption="1syy, resolution 1.70Å" /> | ||
'''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 | + | 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:// | + | 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]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:07:27 2008'' |
Revision as of 13:07, 21 February 2008
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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 with and 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
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