7z0s
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7z0s]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z0S FirstGlance]. <br> | <table><tr><td colspan='2'>[[7z0s]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z0S FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=DR9:1-CIS-9-OCTADECANOYL-2-CIS-9-HEXADECANOYL+PHOSPHATIDYL+GLYCEROL'>DR9</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=LMN:LAURYL+MALTOSE+NEOPENTYL+GLYCOL'>LMN</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=DR9:1-CIS-9-OCTADECANOYL-2-CIS-9-HEXADECANOYL+PHOSPHATIDYL+GLYCEROL'>DR9</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=LMN:LAURYL+MALTOSE+NEOPENTYL+GLYCOL'>LMN</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=7z0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z0s OCA], [https://pdbe.org/7z0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z0s RCSB], [https://www.ebi.ac.uk/pdbsum/7z0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z0s ProSAT]</span></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=7z0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z0s OCA], [https://pdbe.org/7z0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z0s RCSB], [https://www.ebi.ac.uk/pdbsum/7z0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z0s ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/HYCC_ECOLI HYCC_ECOLI] | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase to proton reduction at a [NiFe] hydrogenase. It is of intense interest due to its ability to efficiently produce | + | The prototypical hydrogen-producing enzyme, the membrane-bound formate hydrogenlyase (FHL) complex from Escherichia coli, links formate oxidation at a molybdopterin-containing formate dehydrogenase to proton reduction at a [NiFe] hydrogenase. It is of intense interest due to its ability to efficiently produce H(2) during fermentation, its reversibility, allowing H(2)-dependent CO(2) reduction, and its evolutionary link to respiratory complex I. FHL has been studied for over a century, but its atomic structure remains unknown. Here we report cryo-EM structures of FHL in its aerobically and anaerobically isolated forms at resolutions reaching 2.6 A. This includes well-resolved density for conserved loops linking the soluble and membrane arms believed to be essential in coupling enzymatic turnover to ion translocation across the membrane in the complex I superfamily. We evaluate possible structural determinants of the bias toward hydrogen production over its oxidation and describe an unpredicted metal-binding site near the interface of FdhF and HycF subunits that may play a role in redox-dependent regulation of FdhF interaction with the complex. |
Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli.,Steinhilper R, Hoff G, Heider J, Murphy BJ Nat Commun. 2022 Sep 14;13(1):5395. doi: 10.1038/s41467-022-32831-x. PMID:36104349<ref>PMID:36104349</ref> | Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli.,Steinhilper R, Hoff G, Heider J, Murphy BJ Nat Commun. 2022 Sep 14;13(1):5395. doi: 10.1038/s41467-022-32831-x. PMID:36104349<ref>PMID:36104349</ref> | ||
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</div> | </div> | ||
<div class="pdbe-citations 7z0s" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7z0s" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Formate dehydrogenase 3D structures|Formate dehydrogenase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure of the Escherichia coli formate hydrogenlyase complex (anaerobic preparation, without formate dehydrogenase H)
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