6ohl: Difference between revisions
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The | ==Crystal structure of Fusobacterium nucleatum flavodoxin bound to flavin mononucleotide== | ||
<StructureSection load='6ohl' size='340' side='right'caption='[[6ohl]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== 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> | |||
</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> | |||
<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> | |||
</table> | |||
== Function == | |||
[[http://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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 6ohl" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Kolesnikov, M]] | [[Category: Kolesnikov, M]] | ||
[[Category: Murphy, M E.P]] | |||
[[Category: Electron transfer]] | |||
[[Category: Electron transport]] | |||
[[Category: Flavin mononucleotide]] | |||
[[Category: Flavodoxin]] | |||
[[Category: Reduction potential]] | |||
