6ehs: Difference between revisions

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'''Unreleased structure'''


The entry 6ehs is ON HOLD
==E. coli Hydrogenase-2 chemically reduced structure==
<StructureSection load='6ehs' size='340' side='right'caption='[[6ehs]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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='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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B7LGE4_ECO55 B7LGE4_ECO55]
<div style="background-color:#fffaf0;">
== 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.


Authors:  
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<ref>PMID:29555844</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6ehs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Armstrong FA]]
[[Category: Beaton SE]]
[[Category: Carr SB]]
[[Category: Evans RM]]
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