9r5l: Difference between revisions
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==Crystal structure of class Ie ribonucleotide reductase R2 subunit from Mesoplasma florum with a D212N mutation== | |||
<StructureSection load='9r5l' size='340' side='right'caption='[[9r5l]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9r5l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesoplasma_florum_L1 Mesoplasma florum L1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9R5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9R5L 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]] 1.7Å</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=9r5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9r5l OCA], [https://pdbe.org/9r5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9r5l RCSB], [https://www.ebi.ac.uk/pdbsum/9r5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9r5l ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6F0T5_MESFL Q6F0T5_MESFL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotide (RNA) to deoxyribonucleotide (DNA) building blocks initiated by a long-range (>30 A) proton-coupled electron transfer (PCET) by mechanistic principles that remain much debated. By combining multiscale quantum and classical simulations with directed mutagenesis, X-ray crystallography, and vibrational and electron paramagnetic resonance spectroscopy, we elucidate here the molecular principles underlying how metal-free RNRs initiate the long-range PCET process by creating a highly stable 3,4-dihydroxyphenylalanine (DOPA) initiator radical. We show that DOPA* is redox-tuned by a low-barrier hydrogen bond (LBHB), with a delocalized proton that provides the catalytic power for the ribonucleotide reduction. We find that the LBHB couples to an extended hydrogen-bonded network, with distant mutations resulting in the loss of radical formation, and providing key molecular insight into the long-range radical transport mechanism in RNRs. On a general level, our findings support the direct involvement of LBHB in protein chemistry and the importance of quantum effects in enzyme catalysis. | |||
Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase.,Sirohiwal A, John J, Kutin Y, Kumar R, Baserga F, Srinivas V, Lebrette H, Poverlein MC, Gamiz-Hernandez AP, Heberle J, Kasanmascheff M, Hogbom M, Kaila VRI Proc Natl Acad Sci U S A. 2026 May 12;123(19):e2529856123. doi: , 10.1073/pnas.2529856123. Epub 2026 May 7. PMID:42096306<ref>PMID:42096306</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9r5l" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mesoplasma florum L1]] | |||
[[Category: Hogbom M]] | |||
[[Category: John J]] | |||
Latest revision as of 11:43, 24 May 2026
Crystal structure of class Ie ribonucleotide reductase R2 subunit from Mesoplasma florum with a D212N mutation
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