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| | ==Ribonucleotide Reductase class Ie R2 from Mesoplasma florum, DOPA-active form== | | ==Ribonucleotide Reductase class Ie R2 from Mesoplasma florum, DOPA-active form== |
| - | <StructureSection load='6gp2' size='340' side='right' caption='[[6gp2]], [[Resolution|resolution]] 1.48Å' scene=''> | + | <StructureSection load='6gp2' size='340' side='right'caption='[[6gp2]], [[Resolution|resolution]] 1.48Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gp2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acholeplasma_florum Acholeplasma florum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GP2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gp2]] is a 2 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=6GP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GP2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DAH:3,4-DIHYDROXYPHENYLALANINE'>DAH</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gp3|6gp3]]</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=6gp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gp2 OCA], [https://pdbe.org/6gp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gp2 RCSB], [https://www.ebi.ac.uk/pdbsum/6gp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gp2 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mfl530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=265311 Acholeplasma florum])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gp2 OCA], [http://pdbe.org/6gp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gp2 RCSB], [http://www.ebi.ac.uk/pdbsum/6gp2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gp2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6F0T5_MESFL Q6F0T5_MESFL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6gp2" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6gp2" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acholeplasma florum]] | + | [[Category: Large Structures]] |
| - | [[Category: Branca, R M.M]] | + | [[Category: Mesoplasma florum L1]] |
| - | [[Category: Cox, N]] | + | [[Category: Branca RMM]] |
| - | [[Category: Enrich, J]] | + | [[Category: Cox N]] |
| - | [[Category: Hogbom, M]] | + | [[Category: Enrich J]] |
| - | [[Category: Kutin, Y]] | + | [[Category: Hogbom M]] |
| - | [[Category: Lebrette, H]] | + | [[Category: Kutin Y]] |
| - | [[Category: Lerche, M]] | + | [[Category: Lebrette H]] |
| - | [[Category: Lundin, D]] | + | [[Category: Lerche M]] |
| - | [[Category: Sahlin, M]] | + | [[Category: Lundin D]] |
| - | [[Category: Sjoberg, B M]] | + | [[Category: Sahlin M]] |
| - | [[Category: Srinivas, V]] | + | [[Category: Sjoberg BM]] |
| - | [[Category: Dopa modification]]
| + | [[Category: Srinivas V]] |
| - | [[Category: Ferritin-like superfamily]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Ribonucleotide reduction]]
| + | |
| - | [[Category: Subunit beta]]
| + | |
| Structural highlights
Function
Q6F0T5_MESFL
Publication Abstract from PubMed
Ribonucleotide reductase (RNR) catalyses the only known de novo pathway for the production of all four deoxyribonucleotides that are required for DNA synthesis(1,2). It is essential for all organisms that use DNA as their genetic material and is a current drug target(3,4). Since the discovery that iron is required for function in the aerobic, class I RNR found in all eukaryotes and many bacteria, a dinuclear metal site has been viewed as necessary to generate and stabilize the catalytic radical that is essential for RNR activity(5-7). Here we describe a group of RNR proteins in Mollicutes-including Mycoplasma pathogens-that possess a metal-independent stable radical residing on a modified tyrosyl residue. Structural, biochemical and spectroscopic characterization reveal a stable 3,4-dihydroxyphenylalanine (DOPA) radical species that directly supports ribonucleotide reduction in vitro and in vivo. This observation overturns the presumed requirement for a dinuclear metal site in aerobic ribonucleotide reductase. The metal-independent radical requires new mechanisms for radical generation and stabilization, processes that are targeted by RNR inhibitors. It is possible that this RNR variant provides an advantage under metal starvation induced by the immune system. Organisms that encode this type of RNR-some of which are developing resistance to antibiotics-are involved in diseases of the respiratory, urinary and genital tracts. Further characterization of this RNR family and its mechanism of cofactor generation will provide insight into new enzymatic chemistry and be of value in devising strategies to combat the pathogens that utilize it. We propose that this RNR subclass is denoted class Ie.
Metal-free ribonucleotide reduction powered by a DOPA radical in Mycoplasma pathogens.,Srinivas V, Lebrette H, Lundin D, Kutin Y, Sahlin M, Lerche M, Eirich J, Branca RMM, Cox N, Sjoberg BM, Hogbom M Nature. 2018 Nov;563(7731):416-420. doi: 10.1038/s41586-018-0653-6. Epub 2018 Oct, 31. PMID:30429545[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Srinivas V, Lebrette H, Lundin D, Kutin Y, Sahlin M, Lerche M, Eirich J, Branca RMM, Cox N, Sjoberg BM, Hogbom M. Metal-free ribonucleotide reduction powered by a DOPA radical in Mycoplasma pathogens. Nature. 2018 Nov;563(7731):416-420. doi: 10.1038/s41586-018-0653-6. Epub 2018 Oct, 31. PMID:30429545 doi:http://dx.doi.org/10.1038/s41586-018-0653-6
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