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| | <StructureSection load='5aa5' size='340' side='right'caption='[[5aa5]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5aa5' size='340' side='right'caption='[[5aa5]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5aa5]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AA5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5aa5]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator_H16 Cupriavidus necator H16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AA5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NFU:FORMYL[BIS(HYDROCYANATO-1KAPPAC)]IRONNICKEL(FE-NI)'>NFU</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]] 2.497Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NFU:FORMYL[BIS(HYDROCYANATO-1KAPPAC)]IRONNICKEL(FE-NI)'>NFU</scene></td></tr> |
| - | <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=5aa5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa5 OCA], [http://pdbe.org/5aa5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aa5 RCSB], [http://www.ebi.ac.uk/pdbsum/5aa5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aa5 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=5aa5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa5 OCA], [https://pdbe.org/5aa5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aa5 RCSB], [https://www.ebi.ac.uk/pdbsum/5aa5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aa5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7WXQ4_CUPNH Q7WXQ4_CUPNH] |
| | <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: Cupriavidus necator]] | + | [[Category: Cupriavidus necator H16]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bommer, M]] | + | [[Category: Bommer M]] |
| - | [[Category: Dobbek, H]] | + | [[Category: Dobbek H]] |
| - | [[Category: Hennig, S]] | + | [[Category: Hennig S]] |
| - | [[Category: Jeoung, J H]] | + | [[Category: Jeoung JH]] |
| - | [[Category: Lenz, O]] | + | [[Category: Lenz O]] |
| - | [[Category: Schaefer, C]] | + | [[Category: Schaefer C]] |
| - | [[Category: Dihydrogen]]
| + | |
| - | [[Category: Hydrogenase]]
| + | |
| - | [[Category: Metalloenzyme]]
| + | |
| - | [[Category: Nickel]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygen tolerance]]
| + | |
| - | [[Category: Tropospheric hydrogen]]
| + | |
| Structural highlights
Function
Q7WXQ4_CUPNH
Publication Abstract from PubMed
A novel group of bacterial [NiFe]-hydrogenases is responsible for high-affinity H2 uptake from the troposphere, and is therefore thought to play an important role in the global H2 cycle. Here we present the first crystal structure at 2.85-A resolution of such an actinobacterial-type hydrogenase (AH), which was isolated from the dihydrogen oxidizing bacterium, Ralstonia eutropha. The enzyme has a dimeric structure carrying two active [NiFe] sites that are interconnected by six [4Fe4S] clusters over a range of approximately 90 A. Unlike most other [NiFe]-hydrogenases, the [4Fe4S] cluster proximal to the [NiFe] site is coordinated by three cysteines and one aspartate. Mutagenesis experiments revealed that this aspartate residue is related to the apparent O2 insensitivity of the AH. Our data provide first structural insight into specialized hydrogenases that are supposed to consume atmospheric H2 under challenging conditions, i.e. at high O2 concentration and wide temperature and pH ranges.
Structure of an Actinobacterial-Type [NiFe]-Hydrogenase Reveals Insight into O-Tolerant H Oxidation.,Schafer C, Bommer M, Hennig SE, Jeoung JH, Dobbek H, Lenz O Structure. 2015 Dec 29. pii: S0969-2126(15)00499-2. doi:, 10.1016/j.str.2015.11.010. PMID:26749450[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schafer C, Bommer M, Hennig SE, Jeoung JH, Dobbek H, Lenz O. Structure of an Actinobacterial-Type [NiFe]-Hydrogenase Reveals Insight into O-Tolerant H Oxidation. Structure. 2015 Dec 29. pii: S0969-2126(15)00499-2. doi:, 10.1016/j.str.2015.11.010. PMID:26749450 doi:http://dx.doi.org/10.1016/j.str.2015.11.010
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