6w4x: Difference between revisions
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<StructureSection load='6w4x' size='340' side='right'caption='[[6w4x]], [[Resolution|resolution]] 3.60Å' scene=''> | <StructureSection load='6w4x' size='340' side='right'caption='[[6w4x]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6w4x]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W4X OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6w4x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W4X FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=FY3:2,3,5-TRIFLUORO-L-TYROSINE'>FY3</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</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=6w4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w4x OCA], [https://pdbe.org/6w4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w4x RCSB], [https://www.ebi.ac.uk/pdbsum/6w4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w4x ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RIR1_ECOLI RIR1_ECOLI] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 6w4x" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6w4x" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Drennan CL]] | |||
[[Category: Drennan | [[Category: Kang G]] | ||
[[Category: Kang | [[Category: Stubbe J]] | ||
[[Category: Stubbe | [[Category: Taguchi A]] | ||
[[Category: Taguchi | |||
Latest revision as of 08:21, 25 September 2024
Holocomplex of E. coli class Ia ribonucleotide reductase with GDP and TTPHolocomplex of E. coli class Ia ribonucleotide reductase with GDP and TTP
Structural highlights
FunctionRIR1_ECOLI Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines. Publication Abstract from PubMedRibonucleotide reductases (RNRs) are a diverse family of enzymes that are alone capable of generating 2'-deoxynucleotides de novo and are thus critical in DNA biosynthesis and repair. The nucleotide reduction reaction in all RNRs requires the generation of a transient active site thiyl radical, and in class I RNRs this process involves a long-range radical transfer between two subunits, alpha and beta. Due to the transient subunit association, an atomic resolution structure of an active alpha2beta2 RNR complex has been elusive. Here we use a doubly-substituted beta2, E52Q/(2,3,5)-trifluorotyrosine122-beta2 to trap wildtype-alpha2 in long-lived alpha2beta2 complex. We report the structure of this complex by cryo-electron microscopy to 3.6-A resolution, allowing for structural visualization of a 32-A-long radical transfer pathway that affords RNR activity. Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex.,Kang G, Taguchi AT, Stubbe J, Drennan CL Science. 2020 Mar 26. pii: science.aba6794. doi: 10.1126/science.aba6794. PMID:32217749[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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