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| <StructureSection load='6ohl' size='340' side='right'caption='[[6ohl]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='6ohl' size='340' side='right'caption='[[6ohl]], [[Resolution|resolution]] 1.85Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6ohl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fusiformis"_veillon_and_zuber_1898 "bacillus fusiformis" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OHL FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6ohl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusobacterium_nucleatum Fusobacterium nucleatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OHL FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.85Å</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=6ohl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ohl OCA], [http://pdbe.org/6ohl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ohl RCSB], [http://www.ebi.ac.uk/pdbsum/6ohl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ohl ProSAT]</span></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6ohl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ohl OCA], [https://pdbe.org/6ohl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ohl RCSB], [https://www.ebi.ac.uk/pdbsum/6ohl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ohl ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/Q8RFH4_FUSNN Q8RFH4_FUSNN]] Low-potential electron donor to a number of redox enzymes.[PIRNR:PIRNR038996] | | [https://www.uniprot.org/uniprot/Q8RFH4_FUSNN Q8RFH4_FUSNN] Low-potential electron donor to a number of redox enzymes.[PIRNR:PIRNR038996] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Flavodoxins are small FMN-containing proteins that mediate a variety of electron transfer processes. The primary sequence of flavodoxin from Fusobacterium nucleatum, a pathogenic oral bacterium, is marked with a number of distinct features including a glycine to lysine (K13) substitution in the highly conserved phosphate binding loop (T/S-X-T-G-X-T), variation in the aromatic residues that sandwich the FMN cofactor, and a more even distribution of acidic and basic residues. The Eox/sq (oxidized/semiquinone; -43 mV) and Esq/hq (semiquinone/hydroquinone; -256 mV) are the highest recorded reduction potentials of known long-chain flavodoxins. These more electropositive values are a consequence of the apoprotein binding to the FMN hydroquinone anion with ~70-fold greater affinity compared to the oxidized form of the cofactor. Inspection of the FnFld crystal structure revealed the absence of a hydrogen bond between the protein and the oxidized FMN N5 atom, which likely accounts for the more electropositive Eox/sq . The more electropositive Esq/hq is likely attributed to only one negatively charged group positioned within 12 a of the FMN N1. We show that natural substitutions of highly conserved residues partially account for these more electropositive reduction potentials. This article is protected by copyright. All rights reserved.
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| Structural insight into the high reduction potentials observed for Fusobacterium nucleatum flavodoxin.,Mothersole RG, MacDonald M, Kolesnikov M, Murphy MEP, Wolthers KR Protein Sci. 2019 May 22. doi: 10.1002/pro.3661. PMID:31116469<ref>PMID:31116469</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6ohl" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Flavodoxin 3D structures|Flavodoxin 3D structures]] | | *[[Flavodoxin 3D structures|Flavodoxin 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus fusiformis veillon and zuber 1898]] | | [[Category: Fusobacterium nucleatum]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Kolesnikov, M]] | | [[Category: Kolesnikov M]] |
| [[Category: Murphy, M E.P]] | | [[Category: Murphy MEP]] |
| [[Category: Electron transfer]]
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| [[Category: Electron transport]]
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| [[Category: Flavin mononucleotide]]
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| [[Category: Flavodoxin]]
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| [[Category: Reduction potential]]
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