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| | ==E. coli Hydrogenase-2 (hydrogen reduced form)== | | ==E. coli Hydrogenase-2 (hydrogen reduced form)== |
| - | <StructureSection load='6en9' size='340' side='right' caption='[[6en9]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='6en9' size='340' side='right'caption='[[6en9]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6en9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EN9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6en9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EN9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ehq|6ehq]], [[6ehs|6ehs]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hybO, yghV, b2997, JW2965 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), hybC, b2994, JW2962 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6en9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6en9 OCA], [https://pdbe.org/6en9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6en9 RCSB], [https://www.ebi.ac.uk/pdbsum/6en9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6en9 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>
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| - | <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=6en9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6en9 OCA], [http://pdbe.org/6en9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6en9 RCSB], [http://www.ebi.ac.uk/pdbsum/6en9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6en9 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/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. |
| | <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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Armstrong, F A]] | + | [[Category: Large Structures]] |
| - | [[Category: Beaton, S E]] | + | [[Category: Armstrong FA]] |
| - | [[Category: Carr, S B]] | + | [[Category: Beaton SE]] |
| - | [[Category: Evans, R M]] | + | [[Category: Carr SB]] |
| - | [[Category: Hydrogen oxidation]] | + | [[Category: Evans RM]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Nife hydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
MBHT_ECOLI This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake.
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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