6ohl: Difference between revisions

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<StructureSection load='6ohl' size='340' side='right'caption='[[6ohl]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='6ohl' size='340' side='right'caption='[[6ohl]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ohl]] is a 1 chain structure. 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]] 1.85&#8491;</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;">
== Publication Abstract from PubMed ==
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.


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>
==See Also==
 
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ohl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[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]]
[[Category: Electron transport]]
[[Category: Flavin mononucleotide]]
[[Category: Flavodoxin]]
[[Category: Reduction potential]]

Latest revision as of 17:52, 13 March 2024

Crystal structure of Fusobacterium nucleatum flavodoxin bound to flavin mononucleotideCrystal structure of Fusobacterium nucleatum flavodoxin bound to flavin mononucleotide

Structural highlights

6ohl is a 1 chain structure with sequence from Fusobacterium nucleatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8RFH4_FUSNN Low-potential electron donor to a number of redox enzymes.[PIRNR:PIRNR038996]

See Also

6ohl, resolution 1.85Å

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