5ci4: Difference between revisions
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<StructureSection load='5ci4' size='340' side='right'caption='[[5ci4]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='5ci4' size='340' side='right'caption='[[5ci4]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ci4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ci4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_1303 Escherichia coli 1303]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CI4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><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=SO4:SULFATE+ION'>SO4</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=5ci4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ci4 OCA], [https://pdbe.org/5ci4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ci4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ci4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ci4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0E1LZC3_ECOLX A0A0E1LZC3_ECOLX] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Ribonucleotide reductase|Ribonucleotide reductase]] | *[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Escherichia coli 1303]] | [[Category: Escherichia coli 1303]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Drennan CL]] | |||
[[Category: Drennan | [[Category: Funk MA]] | ||
[[Category: Funk | |||
Revision as of 15:07, 14 June 2023
Ribonucleotide reductase beta subunitRibonucleotide reductase beta subunit
Structural highlights
FunctionPublication Abstract from PubMedFluorinated tyrosines (FnY's, n = 2 and 3) have been site-specifically incorporated into E. coli class Ia ribonucleotide reductase (RNR) using the recently evolved M. jannaschii Y-tRNA synthetase/tRNA pair. Class Ia RNRs require four redox active Y's, a stable Y radical (Y.) in the beta subunit (position 122 in E. coli), and three transiently oxidized Y's (356 in beta and 731 and 730 in alpha) to initiate the radical-dependent nucleotide reduction process. FnY (3,5; 2,3; 2,3,5; and 2,3,6) incorporation in place of Y122-beta and the X-ray structures of each resulting beta with a diferric cluster are reported and compared with wt-beta2 crystallized under the same conditions. The essential diferric-FnY. cofactor is self-assembled from apo FnY-beta2, Fe2+, and O2 to produce approximately 1 Y./beta2 and approximately 3 Fe3+/beta2. The FnY. are stable and active in nucleotide reduction with activities that vary from 5% to 85% that of wt-beta2. Each FnY.-beta2 has been characterized by 9 and 130 GHz electron paramagnetic resonance and high-field electron nuclear double resonance spectroscopies. The hyperfine interactions associated with the 19F nucleus provide unique signatures of each FnY. that are readily distinguishable from unlabeled Y.'s. The variability of the abiotic FnY pKa's (6.4 to 7.8) and reduction potentials (-30 to +130 mV relative to Y at pH 7.5) provide probes of enzymatic reactions proposed to involve Y.'s in catalysis and to investigate the importance and identity of hopping Y.'s within redox active proteins proposed to protect them from uncoupled radical chemistry. Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example.,Oyala PH, Ravichandran KR, Funk MA, Stucky PA, Stich TA, Drennan CL, Britt RD, Stubbe J J Am Chem Soc. 2016 Jun 21. PMID:27276098[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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