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6ohk

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Current revision (14:52, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6ohk' size='340' side='right'caption='[[6ohk]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
<StructureSection load='6ohk' size='340' side='right'caption='[[6ohk]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ohk]] 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=6OHK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OHK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ohk]] 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=6OHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OHK FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<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=6ohk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ohk OCA], [http://pdbe.org/6ohk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ohk RCSB], [http://www.ebi.ac.uk/pdbsum/6ohk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ohk ProSAT]</span></td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ohk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ohk OCA], [https://pdbe.org/6ohk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ohk RCSB], [https://www.ebi.ac.uk/pdbsum/6ohk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ohk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q8RFH4_FUSNN Q8RFH4_FUSNN]] Low-potential electron donor to a number of redox enzymes.[PIRNR:PIRNR038996]
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[https://www.uniprot.org/uniprot/Q8RFH4_FUSNN Q8RFH4_FUSNN] Low-potential electron donor to a number of redox enzymes.[PIRNR:PIRNR038996]
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<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ohk" 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]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus fusiformis veillon and zuber 1898]]
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[[Category: Fusobacterium nucleatum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kolesnikov, M]]
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[[Category: Kolesnikov M]]
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[[Category: Murphy, M E.P]]
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[[Category: Murphy MEP]]
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[[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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Current revision

Crystal structure of Fusobacterium nucleatum flavodoxin mutant K13G bound to flavin mononucleotide

PDB ID 6ohk

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