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6tjr
From Proteopedia
(Difference between revisions)
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==Structure of HdrA-like subunit from Hyphomicrobium denitrificans== | ==Structure of HdrA-like subunit from Hyphomicrobium denitrificans== | ||
| - | <StructureSection load='6tjr' size='340' side='right'caption='[[6tjr]]' scene=''> | + | <StructureSection load='6tjr' size='340' side='right'caption='[[6tjr]], [[Resolution|resolution]] 1.43Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TJR OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6tjr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_51888 Atcc 51888]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TJR FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hden_0691 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53399 ATCC 51888])</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=6tjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tjr OCA], [https://pdbe.org/6tjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tjr RCSB], [https://www.ebi.ac.uk/pdbsum/6tjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tjr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many Bacteria and Archaea employ a novel pathway of sulfur oxidation involving an enzyme complex that is related to the heterodisulfide reductase (HdrABC) of methanogens. As a first step in the biochemical characterization of Hdr-like proteins from sulfur oxidizers (sHdr), we structurally analyzed the recombinant sHdrA protein from the Alphaproteobacterium Hyphomicrobium denitrificans at 1.4 A resolution. The sHdrA core structure is similar to that of methanogenic HdrA (mHdrA) which binds the electron-bifurcating flavin adenine dinucleotide (FAD), the heart of the HdrABC-[NiFe]-hydrogenase catalyzed reaction. Each sHdrA homodimer carries two FADs and two [4Fe-4S] clusters being linked by electron conductivity. Redox titrations monitored by electron paramagnetic resonance and visible spectroscopy revealed a redox potential between -203 and -188 mV for the [4Fe-4S] center. The potentials for the FADH*/FADH(-) and FAD/FADH* pairs reside between -174 and -156 mV and between -81 and -19 mV, respectively. The resulting stable semiquinone FADH* species, already detectable in the visible and EPR spectra of the as-isolated state of sHdrA is incompatible with basic principles of flavin-based electron bifurcation such that the sHdr complex does not apply this new mode of energy coupling. The inverted one-electron FAD redox potentials of sHdr and mHdr are clearly reflected in the different FAD-polypeptide interactions. According to this finding and the assumption that the sHdr complex forms an asymmetric HdrAA'B1C1B2C2 hexamer we tentatively propose a mechanism that links protein-bound sulfane oxidation to sulfite on HdrB1 with NAD(+) reduction via lipoamide disulfide reduction on HdrB2. The FAD of HdrA thereby serves as an electron storage unit. | ||
| + | |||
| + | Structural and spectroscopic characterization of a HdrA-like subunit from Hyphomicrobium denitrificans.,Ernst C, Kayastha K, Koch T, Venceslau SS, Pereira IAC, Demmer U, Ermler U, Dahl C FEBS J. 2020 Aug 4. doi: 10.1111/febs.15505. PMID:32750208<ref>PMID:32750208</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6tjr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 51888]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dahl C]] | + | [[Category: Dahl, C]] |
| - | [[Category: Ermler U]] | + | [[Category: Ermler, U]] |
| - | [[Category: Kayastha K]] | + | [[Category: Kayastha, K]] |
| + | [[Category: Dissimilatory sulfur oxidation]] | ||
| + | [[Category: Electron bifurcation]] | ||
| + | [[Category: Fad]] | ||
| + | [[Category: Flavoprotein]] | ||
| + | [[Category: Heterodisulfide reductase]] | ||
Current revision
Structure of HdrA-like subunit from Hyphomicrobium denitrificans
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