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New page: left|200px<br /><applet load="1mrr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mrr, resolution 2.5Å" /> '''SUBSTITUTION OF MANGA...
 
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[[Image:1mrr.gif|left|200px]]<br /><applet load="1mrr" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mrr, resolution 2.5&Aring;" />
'''SUBSTITUTION OF MANGANESE FOR IRON IN RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI. SPECTROSCOPIC AND CRYSTALLOGRAPHIC CHARACTERIZATION'''<br />


==Overview==
==SUBSTITUTION OF MANGANESE FOR IRON IN RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI. SPECTROSCOPIC AND CRYSTALLOGRAPHIC CHARACTERIZATION==
Each polypeptide chain of protein R2, the small subunit of ribonucleotide, reductase from Escherichia coli, contains a stable tyrosyl radical and two, antiferromagnetically coupled oxo-bridged ferric ions. A refined structure, of R2 has been recently obtained. R2 can be converted into apoR2 by, chelating out the metal cofactor and scavenging the radical. This study, shows that apoR2 has a very strong affinity for four stable Mn2+ ions. The, manganese-containing form of R2, named Mn-R2, has been studied by EPR, spectroscopy and x-ray crystallography. It contains two binuclear, manganese clusters in which the two manganese ions occupy the natural, iron-binding sites and are only bridged by carboxylates from glutamates, 115 and 238. This in turn explains why the spin-exchange interaction, between the two ions is very weak and why Mn-R2 is EPR active. Mn-R2 could, provide a model for the native diferrous form of protein R2, and a, detailed molecular mechanism for the reduction of the iron center of, protein R2 is proposed.
<StructureSection load='1mrr' size='340' side='right'caption='[[1mrr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mrr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MRR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=1mrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mrr OCA], [https://pdbe.org/1mrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mrr RCSB], [https://www.ebi.ac.uk/pdbsum/1mrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mrr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RIR2_ECOLI RIR2_ECOLI] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mr/1mrr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1mrr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Each polypeptide chain of protein R2, the small subunit of ribonucleotide reductase from Escherichia coli, contains a stable tyrosyl radical and two antiferromagnetically coupled oxo-bridged ferric ions. A refined structure of R2 has been recently obtained. R2 can be converted into apoR2 by chelating out the metal cofactor and scavenging the radical. This study shows that apoR2 has a very strong affinity for four stable Mn2+ ions. The manganese-containing form of R2, named Mn-R2, has been studied by EPR spectroscopy and x-ray crystallography. It contains two binuclear manganese clusters in which the two manganese ions occupy the natural iron-binding sites and are only bridged by carboxylates from glutamates 115 and 238. This in turn explains why the spin-exchange interaction between the two ions is very weak and why Mn-R2 is EPR active. Mn-R2 could provide a model for the native diferrous form of protein R2, and a detailed molecular mechanism for the reduction of the iron center of protein R2 is proposed.


==About this Structure==
Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterization.,Atta M, Nordlund P, Aberg A, Eklund H, Fontecave M J Biol Chem. 1992 Oct 15;267(29):20682-8. PMID:1328209<ref>PMID:1328209</ref>
1MRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN and HG 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=1MRR OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterization., Atta M, Nordlund P, Aberg A, Eklund H, Fontecave M, J Biol Chem. 1992 Oct 15;267(29):20682-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1328209 1328209]
</div>
<div class="pdbe-citations 1mrr" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Ribonucleoside-diphosphate reductase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Eklund H]]
[[Category: Eklund, H.]]
[[Category: Nordlund P]]
[[Category: Nordlund, P.]]
[[Category: HG]]
[[Category: MN]]
[[Category: reductase(acting on ch2)]]
 
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