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==Crystal structure of the F127Y mutant of Ribonucleotide Reductase R2 from Chlamydia trachomatis==
==Crystal structure of the F127Y mutant of Ribonucleotide Reductase R2 from Chlamydia trachomatis==
<StructureSection load='2ani' size='340' side='right' caption='[[2ani]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2ani' size='340' side='right'caption='[[2ani]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ani]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"chlamydozoon_trachomatis"_(busacca_1935)_moshkovski_1945 "chlamydozoon trachomatis" (busacca 1935) moshkovski 1945]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANI FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ani]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ANI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1syy|1syy]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nrdB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=813 "Chlamydozoon trachomatis" (Busacca 1935) Moshkovski 1945])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ani FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ani OCA], [https://pdbe.org/2ani PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ani RCSB], [https://www.ebi.ac.uk/pdbsum/2ani PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ani ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ani FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ani OCA], [http://pdbe.org/2ani PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ani RCSB], [http://www.ebi.ac.uk/pdbsum/2ani PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ani ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RIR2_CHLTR RIR2_CHLTR]] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).  
[https://www.uniprot.org/uniprot/RIR2_CHLTR RIR2_CHLTR] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ani ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ani ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A recently discovered subgroup of class I ribonucleotide reductase (RNR) found in the infectious bacterium Chlamydia trachomatis (C. trachomatis) was shown to exhibit a high-valent Fe(III)Fe(IV) center instead of the tyrosyl radical observed normally in all class I RNRs. The X-ray structure showed that C. trachomatis WT RNR has a phenylalanine at the position of the active tyrosine in Escherichia coli RNR. In this paper the X-ray structure of variant F127Y is presented, where the tyrosine is restored. Using (1)H- and (57)Fe-ENDOR spectroscopy it is shown, that in WT and variants F127Y and Y129F of C. trachomatis RNR, the Fe(III)Fe(IV) center is virtually identical with the short-lived intermediate X observed during the iron oxygen reconstitution reaction in class I RNR from E. coli. The experimental data are consistent with a recent theoretical model for X, proposing two bridging oxo ligands and one terminal water ligand. A surprising extension of the lifetime of the Fe(III)Fe(IV) state in C. trachomatis from a few seconds to several hours at room temperature was observed under catalytic conditions in the presence of substrate. These findings suggest a possible new role for the Fe(III)Fe(IV) state also in other class I RNR, during the catalytic radical transfer reaction, by which the substrate turnover is started.
Structure of the high-valent FeIIIFeIV state in ribonucleotide reductase (RNR) of Chlamydia trachomatis--combined EPR, 57Fe-, 1H-ENDOR and X-ray studies.,Voevodskaya N, Galander M, Hogbom M, Stenmark P, McClarty G, Graslund A, Lendzian F Biochim Biophys Acta. 2007 Oct;1774(10):1254-63. Epub 2007 Jul 17. PMID:17827077<ref>PMID:17827077</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ani" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribonucleotide reductase|Ribonucleotide reductase]]
*[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ribonucleoside-diphosphate reductase]]
[[Category: Chlamydia trachomatis]]
[[Category: Hogbom, M]]
[[Category: Large Structures]]
[[Category: Nordlund, P]]
[[Category: Hogbom M]]
[[Category: Stenmark, P]]
[[Category: Nordlund P]]
[[Category: Diiron]]
[[Category: Stenmark P]]
[[Category: Oxidoreductase]]
[[Category: Radical]]
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