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| | ==Solution Structure of HndAc : A Thioredoxin-like [2Fe-2S] Ferredoxin Involved in the NADP-reducing Hydrogenase Complex== | | ==Solution Structure of HndAc : A Thioredoxin-like [2Fe-2S] Ferredoxin Involved in the NADP-reducing Hydrogenase Complex== |
| - | <StructureSection load='2auv' size='340' side='right'caption='[[2auv]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='2auv' size='340' side='right'caption='[[2auv]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2auv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49200 Atcc 49200]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AUV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AUV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2auv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Solidesulfovibrio_fructosivorans Solidesulfovibrio fructosivorans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AUV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrogen_dehydrogenase_(NADP(+)) Hydrogen dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.1.3 1.12.1.3] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=2auv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2auv OCA], [http://pdbe.org/2auv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2auv RCSB], [http://www.ebi.ac.uk/pdbsum/2auv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2auv 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=2auv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2auv OCA], [https://pdbe.org/2auv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2auv RCSB], [https://www.ebi.ac.uk/pdbsum/2auv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2auv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HNDA_DESFR HNDA_DESFR]] Catalyzes the reduction of NADP in the presence of molecular H(2) to yield NADPH.<ref>PMID:7751270</ref> <ref>PMID:9703971</ref> | + | [https://www.uniprot.org/uniprot/HNDA_SOLFR HNDA_SOLFR] Catalyzes the reduction of NADP in the presence of molecular H(2) to yield NADPH.<ref>PMID:7751270</ref> <ref>PMID:9703971</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 49200]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bornet, O]] | + | [[Category: Solidesulfovibrio fructosivorans]] |
| - | [[Category: Chetrit, B]] | + | [[Category: Bornet O]] |
| - | [[Category: Dermoun, Z]] | + | [[Category: Chetrit B]] |
| - | [[Category: Guerlesquin, F]] | + | [[Category: Dermoun Z]] |
| - | [[Category: Morelli, X]] | + | [[Category: Guerlesquin F]] |
| - | [[Category: Nouailler, M]] | + | [[Category: Morelli X]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Nouailler M]] |
| - | [[Category: Thiordoxin-like]]
| + | |
| - | [[Category: Thioredoxin]]
| + | |
| Structural highlights
Function
HNDA_SOLFR Catalyzes the reduction of NADP in the presence of molecular H(2) to yield NADPH.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The NADP-reducing hydrogenase complex from Desulfovibrio fructosovorans is a heterotetramer encoded by the hndABCD operon. Sequence analysis indicates that the HndC subunit (52 kDa) corresponds to the NADP-reducing unit, and the HndD subunit (63.5 kDa) is homologous to Clostridium pasteurianum hydrogenase. The role of HndA and HndB subunits (18.8 kDa and 13.8 kDa, respectively) in the complex remains unknown. The HndA subunit belongs to the [2Fe-2S] ferredoxin family typified by C. pasteurianum ferredoxin. HndA is organized into two independent structural domains, and we report in the present work the NMR structure of its C-terminal domain, HndAc. HndAc has a thioredoxin-like fold consisting in four beta-strands and two relatively long helices. The [2Fe-2S] cluster is located near the surface of the protein and bound to four cysteine residues particularly well conserved in this class of proteins. Electron exchange between the HndD N-terminal [2Fe-2S] domain (HndDN) and HndAc has been previously evidenced, and in the present studies we have mapped the binding site of the HndDN domain on HndAc. A structural analysis of HndB indicates that it is a FeS subunit with 41% similarity with HndAc and it contains a possible thioredoxin-like fold. Our data let us propose that HndAc and HndB can form a heterodimeric intermediate in the electron transfer between the hydrogenase (HndD) active site and the NADP reduction site in HndC.
Solution structure of HndAc: a thioredoxin-like domain involved in the NADP-reducing hydrogenase complex.,Nouailler M, Morelli X, Bornet O, Chetrit B, Dermoun Z, Guerlesquin F Protein Sci. 2006 Jun;15(6):1369-78. PMID:16731971[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Malki S, Saimmaime I, De Luca G, Rousset M, Dermoun Z, Belaich JP. Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J Bacteriol. 1995 May;177(10):2628-36. PMID:7751270
- ↑ de Luca G, de Philip P, Rousset M, Belaich JP, Dermoun Z. The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity. Biochem Biophys Res Commun. 1998 Jul 30;248(3):591-6. PMID:9703971 doi:http://dx.doi.org/10.1006/bbrc.1998.9022
- ↑ Nouailler M, Morelli X, Bornet O, Chetrit B, Dermoun Z, Guerlesquin F. Solution structure of HndAc: a thioredoxin-like domain involved in the NADP-reducing hydrogenase complex. Protein Sci. 2006 Jun;15(6):1369-78. PMID:16731971 doi:15/6/1369
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