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| | <StructureSection load='6ehs' size='340' side='right'caption='[[6ehs]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='6ehs' size='340' side='right'caption='[[6ehs]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ehs]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EHS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6EHS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ehs]] is a 4 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=6EHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EHS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTN:DITHIONITE'>DTN</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=DTN:DITHIONITE'>DTN</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ehq|6ehq]]</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=6ehs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ehs OCA], [https://pdbe.org/6ehs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ehs RCSB], [https://www.ebi.ac.uk/pdbsum/6ehs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ehs ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogenase_(acceptor) Hydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.99.6 1.12.99.6] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ehs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ehs OCA], [http://pdbe.org/6ehs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ehs RCSB], [http://www.ebi.ac.uk/pdbsum/6ehs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ehs ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MBHT_ECOLI MBHT_ECOLI]] This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake. [[http://www.uniprot.org/uniprot/MBHM_ECOLI MBHM_ECOLI]] This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake. | + | [https://www.uniprot.org/uniprot/B7LGE4_ECO55 B7LGE4_ECO55] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Armstrong, F A]] | + | [[Category: Armstrong FA]] |
| - | [[Category: Beaton, S E]] | + | [[Category: Beaton SE]] |
| - | [[Category: Carr, S B]] | + | [[Category: Carr SB]] |
| - | [[Category: Evans, R M]] | + | [[Category: Evans RM]] |
| - | [[Category: Hydrogen oxidation]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Nife hydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
6ehs is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.5Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
B7LGE4_ECO55
Publication Abstract from PubMed
Under anaerobic conditions, Escherichia coli is able to metabolize molecular hydrogen via the action of several [NiFe]-hydrogenase enzymes. Hydrogenase-2, which is typically present in cells at low levels during anaerobic respiration, is a periplasmic-facing membrane-bound complex that functions as a proton pump to convert energy from hydrogen (H2) oxidation into a proton gradient; consequently, its structure is of great interest. Empirically, the complex consists of a tightly bound core catalytic module, comprising large (HybC) and small (HybO) subunits, which is attached to an Fe-S protein (HybA) and an integral membrane protein (HybB). To date, efforts to gain a more detailed picture have been thwarted by low native expression levels of Hydrogenase-2 and the labile interaction between HybOC and HybA/HybB subunits. In the present paper, we describe a new overexpression system that has facilitated the determination of high-resolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex.
The structure of hydrogenase-2 from Escherichia coli: implications for H2-driven proton pumping.,Beaton SE, Evans RM, Finney AJ, Lamont CM, Armstrong FA, Sargent F, Carr SB Biochem J. 2018 Apr 16;475(7):1353-1370. doi: 10.1042/BCJ20180053. PMID:29555844[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Beaton SE, Evans RM, Finney AJ, Lamont CM, Armstrong FA, Sargent F, Carr SB. The structure of hydrogenase-2 from Escherichia coli: implications for H2-driven proton pumping. Biochem J. 2018 Apr 16;475(7):1353-1370. doi: 10.1042/BCJ20180053. PMID:29555844 doi:http://dx.doi.org/10.1042/BCJ20180053
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