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| | <StructureSection load='5d51' size='340' side='right'caption='[[5d51]], [[Resolution|resolution]] 1.47Å' scene=''> | | <StructureSection load='5d51' size='340' side='right'caption='[[5d51]], [[Resolution|resolution]] 1.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5d51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17697_[[alcaligenes_eutrophus]] Atcc 17697 [[alcaligenes eutrophus]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D51 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D51 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5d51]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D51 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=F4S:FE4-S3+CLUSTER'>F4S</scene>, <scene name='pdbligand=KR:KRYPTON'>KR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NFV:NI-FE+OXIDIZED+ACTIVE+CENTER'>NFV</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=F4S:FE4-S3+CLUSTER'>F4S</scene>, <scene name='pdbligand=KR:KRYPTON'>KR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NFV:NI-FE+OXIDIZED+ACTIVE+CENTER'>NFV</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hoxG, PHG002 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106590 ATCC 17697 [[Alcaligenes eutrophus]]]), hoxK, PHG001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106590 ATCC 17697 [[Alcaligenes eutrophus]]])</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=5d51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d51 OCA], [https://pdbe.org/5d51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d51 RCSB], [https://www.ebi.ac.uk/pdbsum/5d51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d51 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d51 OCA], [http://pdbe.org/5d51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d51 RCSB], [http://www.ebi.ac.uk/pdbsum/5d51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d51 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MBHL_CUPNH MBHL_CUPNH]] This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. [[http://www.uniprot.org/uniprot/MBHS_CUPNH MBHS_CUPNH]] This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. | + | [https://www.uniprot.org/uniprot/MBHL_CUPNH MBHL_CUPNH] This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. |
| | <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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carpentier, P]] | + | [[Category: Carpentier P]] |
| - | [[Category: Frielingsdorf, S]] | + | [[Category: Frielingsdorf S]] |
| - | [[Category: Kalms, J]] | + | [[Category: Kalms J]] |
| - | [[Category: Lenz, O]] | + | [[Category: Lenz O]] |
| - | [[Category: Linden, P van der]]
| + | [[Category: Scheerer P]] |
| - | [[Category: Scheerer, P]] | + | [[Category: Schmidt A]] |
| - | [[Category: Schmidt, A]] | + | [[Category: Van der Linden P]] |
| - | [[Category: Stetten, D von]] | + | [[Category: Von Stetten D]] |
| - | [[Category: Aerobic hydrogen bacteria]] | + | |
| - | [[Category: Bimetallic]]
| + | |
| - | [[Category: Dehydrogenase]]
| + | |
| - | [[Category: Dihydrogen]]
| + | |
| - | [[Category: Gas transport]]
| + | |
| - | [[Category: Hydrogen]]
| + | |
| - | [[Category: Hydrogen catalysis]]
| + | |
| - | [[Category: Hydrophobic tunnel]]
| + | |
| - | [[Category: Iron-sulfur cluster]]
| + | |
| - | [[Category: Knallgasbacteria]]
| + | |
| - | [[Category: Krypton]]
| + | |
| - | [[Category: Membrane-bound]]
| + | |
| - | [[Category: Metalloenzyme]]
| + | |
| - | [[Category: Metalloprotein catalytic center]]
| + | |
| - | [[Category: Ni-fe active site]]
| + | |
| - | [[Category: Nickel-iron cofactor]]
| + | |
| - | [[Category: Noble gas derivatization]]
| + | |
| - | [[Category: Oxidized state]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygen-tolerant hydrogenase]]
| + | |
| - | [[Category: Proteobacteria]]
| + | |
| - | [[Category: T-cluster]]
| + | |
| Structural highlights
5d51 is a 2 chain structure with sequence from Cupriavidus necator. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MBHL_CUPNH This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Publication Abstract from PubMed
[NiFe] hydrogenases are metalloenzymes catalyzing the reversible heterolytic cleavage of hydrogen into protons and electrons. Gas tunnels make the deeply buried active site accessible to substrates and inhibitors. Understanding the architecture and function of the tunnels is pivotal to modulating the feature of O2 tolerance in a subgroup of these [NiFe] hydrogenases, as they are interesting for developments in renewable energy technologies. Here we describe the crystal structure of the O2 -tolerant membrane-bound [NiFe] hydrogenase of Ralstonia eutropha (ReMBH), using krypton-pressurized crystals. The positions of the krypton atoms allow a comprehensive description of the tunnel network within the enzyme. A detailed overview of tunnel sizes, lengths, and routes is presented from tunnel calculations. A comparison of the ReMBH tunnel characteristics with crystal structures of other O2 -tolerant and O2 -sensitive [NiFe] hydrogenases revealed considerable differences in tunnel size and quantity between the two groups, which might be related to the striking feature of O2 tolerance.
Krypton Derivatization of an O2 -Tolerant Membrane-Bound [NiFe] Hydrogenase Reveals a Hydrophobic Tunnel Network for Gas Transport.,Kalms J, Schmidt A, Frielingsdorf S, van der Linden P, von Stetten D, Lenz O, Carpentier P, Scheerer P Angew Chem Int Ed Engl. 2016 Apr 25;55(18):5586-90. doi: 10.1002/anie.201508976. , Epub 2016 Feb 23. PMID:26913499[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kalms J, Schmidt A, Frielingsdorf S, van der Linden P, von Stetten D, Lenz O, Carpentier P, Scheerer P. Krypton Derivatization of an O2 -Tolerant Membrane-Bound [NiFe] Hydrogenase Reveals a Hydrophobic Tunnel Network for Gas Transport. Angew Chem Int Ed Engl. 2016 Apr 25;55(18):5586-90. doi: 10.1002/anie.201508976. , Epub 2016 Feb 23. PMID:26913499 doi:http://dx.doi.org/10.1002/anie.201508976
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