2alx: Difference between revisions
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< | ==Ribonucleotide Reductase R2 from Escherichia coli in space group P6(1)22== | ||
<StructureSection load='2alx' size='340' side='right'caption='[[2alx]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2alx]] is a 1 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=2ALX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ALX FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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=2alx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2alx OCA], [https://pdbe.org/2alx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2alx RCSB], [https://www.ebi.ac.uk/pdbsum/2alx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2alx 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/al/2alx_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2alx ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A new crystal form of wild-type ribonucleotide reductase R2 from Escherichia coli was obtained. Crystals grow in space group P6(1)22 with one R2 monomer in the asymmetric unit. A twofold crystallographic symmetry axis generates the physiological dimeric form of R2. Co-crystallization with CoCl(2) or MnCl(2) results in full occupancy of the dinuclear metal site. The structure of the Mn(II)-loaded form was determined to 2.6 Angstroms resolution by molecular replacement. The crystallization conditions, backbone conformation, crystal-packing interactions and metal centers are compared with those of previously determined crystal forms. | |||
Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122.,Sommerhalter M, Saleh L, Bollinger JM Jr, Rosenzweig AC Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1649-54. Epub 2005, Nov 19. PMID:16301799<ref>PMID:16301799</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2alx" 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: | [[Category: Large Structures]] | ||
[[Category: Jr | [[Category: Bollinger Jr JM]] | ||
[[Category: Rosenzweig | [[Category: Rosenzweig AC]] | ||
[[Category: Saleh | [[Category: Saleh L]] | ||
[[Category: Sommerhalter | [[Category: Sommerhalter M]] | ||
Latest revision as of 10:26, 23 August 2023
Ribonucleotide Reductase R2 from Escherichia coli in space group P6(1)22Ribonucleotide Reductase R2 from Escherichia coli in space group P6(1)22
Structural highlights
FunctionRIR2_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA new crystal form of wild-type ribonucleotide reductase R2 from Escherichia coli was obtained. Crystals grow in space group P6(1)22 with one R2 monomer in the asymmetric unit. A twofold crystallographic symmetry axis generates the physiological dimeric form of R2. Co-crystallization with CoCl(2) or MnCl(2) results in full occupancy of the dinuclear metal site. The structure of the Mn(II)-loaded form was determined to 2.6 Angstroms resolution by molecular replacement. The crystallization conditions, backbone conformation, crystal-packing interactions and metal centers are compared with those of previously determined crystal forms. Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122.,Sommerhalter M, Saleh L, Bollinger JM Jr, Rosenzweig AC Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1649-54. Epub 2005, Nov 19. PMID:16301799[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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