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==Structure of a flavodoxin from the domain Archaea== | |||
<StructureSection load='5wid' size='340' side='right'caption='[[5wid]], [[Resolution|resolution]] 1.68Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5wid]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans_C2A Methanosarcina acetivorans C2A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WID FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.681Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=5wid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wid OCA], [https://pdbe.org/5wid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wid RCSB], [https://www.ebi.ac.uk/pdbsum/5wid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wid ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8TPV5_METAC Q8TPV5_METAC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Flavodoxins, electron transfer proteins essential for diverse metabolisms in microbes from the domain Bacteria, are extensively characterized. Remarkably, although genomic annotations of flavodoxins are widespread in microbes from the domain Archaea, none have been isolated and characterized. Herein is described the structural, biochemical, and physiological characterization of an unusual flavodoxin (FldA) from Methanosarcina acetivorans, an acetate-utilizing methane-producing microbe of the domain Archaea In contrast to all flavodoxins, FldA is homodimeric, markedly less acidic, and stabilizes an anionic semiquinone. The crystal structure reveals an flavin mononucleotide (FMN) binding site unique from all other flavodoxins that provides a rationale for stabilization of the anionic semiquinone and a remarkably low reduction potentials for both the oxidized/semiquinone (-301 mV) and semiquinone/hydroquinone couples (-464 mV). FldA is up-regulated in acetate-grown versus methanol-grown cells and shown here to substitute for ferredoxin in mediating the transfer of low potential electrons from the carbonyl of acetate to the membrane-bound electron transport chain that generates ion gradients driving ATP synthesis. FldA offers potential advantages over ferredoxin by (i) sparing iron for abundant iron-sulfur proteins essential for acetotrophic growth and (ii) resilience to oxidative damage. | |||
Structure and function of an unusual flavodoxin from the domain Archaea.,Prakash D, Iyer PR, Suharti S, Walters KA, Santiago-Martinez MG, Golbeck JH, Murakami KS, Ferry JG Proc Natl Acad Sci U S A. 2019 Dec 17;116(51):25917-25922. doi:, 10.1073/pnas.1908578116. Epub 2019 Dec 4. PMID:31801875<ref>PMID:31801875</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5wid" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanosarcina acetivorans C2A]] | |||
[[Category: Ferry JG]] | |||
[[Category: Murakami KS]] | |||
Latest revision as of 17:13, 4 October 2023
Structure of a flavodoxin from the domain ArchaeaStructure of a flavodoxin from the domain Archaea
Structural highlights
FunctionPublication Abstract from PubMedFlavodoxins, electron transfer proteins essential for diverse metabolisms in microbes from the domain Bacteria, are extensively characterized. Remarkably, although genomic annotations of flavodoxins are widespread in microbes from the domain Archaea, none have been isolated and characterized. Herein is described the structural, biochemical, and physiological characterization of an unusual flavodoxin (FldA) from Methanosarcina acetivorans, an acetate-utilizing methane-producing microbe of the domain Archaea In contrast to all flavodoxins, FldA is homodimeric, markedly less acidic, and stabilizes an anionic semiquinone. The crystal structure reveals an flavin mononucleotide (FMN) binding site unique from all other flavodoxins that provides a rationale for stabilization of the anionic semiquinone and a remarkably low reduction potentials for both the oxidized/semiquinone (-301 mV) and semiquinone/hydroquinone couples (-464 mV). FldA is up-regulated in acetate-grown versus methanol-grown cells and shown here to substitute for ferredoxin in mediating the transfer of low potential electrons from the carbonyl of acetate to the membrane-bound electron transport chain that generates ion gradients driving ATP synthesis. FldA offers potential advantages over ferredoxin by (i) sparing iron for abundant iron-sulfur proteins essential for acetotrophic growth and (ii) resilience to oxidative damage. Structure and function of an unusual flavodoxin from the domain Archaea.,Prakash D, Iyer PR, Suharti S, Walters KA, Santiago-Martinez MG, Golbeck JH, Murakami KS, Ferry JG Proc Natl Acad Sci U S A. 2019 Dec 17;116(51):25917-25922. doi:, 10.1073/pnas.1908578116. Epub 2019 Dec 4. PMID:31801875[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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