1syy

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[[Image:1syy.gif|left|200px]]
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{{STRUCTURE_1syy| PDB=1syy | SCENE= }}
{{STRUCTURE_1syy| PDB=1syy | SCENE= }}
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'''Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis'''
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===Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15247479 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15247479}}
==About this Structure==
==About this Structure==
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[[Category: Iron coupled radical]]
[[Category: Iron coupled radical]]
[[Category: Oxygen activation]]
[[Category: Oxygen activation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:17:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:50:54 2008''

Revision as of 02:50, 28 July 2008

Image:1syy.png

Template:STRUCTURE 1syy

Crystal structure of the R2 subunit of ribonucleotide reductase from Chlamydia trachomatis

Template:ABSTRACT PUBMED 15247479

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

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