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| | ==HADDOCK model of ferredoxin and [FeFe] hydrogenase complex== | | ==HADDOCK model of ferredoxin and [FeFe] hydrogenase complex== |
| - | <StructureSection load='2n0s' size='340' side='right' caption='[[2n0s]], [[NMR_Ensembles_of_Models | 4 NMR models]]' scene=''> | + | <StructureSection load='2n0s' size='340' side='right'caption='[[2n0s]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2n0s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N0S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n0s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N0S 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>, <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">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hyd1, HYD1, hydA, hydA1, CHLREDRAFT_183963 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE]), PETF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</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>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin_hydrogenase Ferredoxin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.7.2 1.12.7.2] </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=2n0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0s OCA], [https://pdbe.org/2n0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n0s RCSB], [https://www.ebi.ac.uk/pdbsum/2n0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0s ProSAT]</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=2n0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0s OCA], [http://pdbe.org/2n0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n0s RCSB], [http://www.ebi.ac.uk/pdbsum/2n0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FER_CHLRE FER_CHLRE]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | + | [https://www.uniprot.org/uniprot/Q9FYU1_CHLRE Q9FYU1_CHLRE] |
| | <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: Chlre]] | + | [[Category: Chlamydomonas reinhardtii]] |
| - | [[Category: Ferredoxin hydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Fares, C]] | + | [[Category: Fares C]] |
| - | [[Category: Lubitz, W]] | + | [[Category: Lubitz W]] |
| - | [[Category: Reijerse, E]] | + | [[Category: Reijerse E]] |
| - | [[Category: Rumpel, S]] | + | [[Category: Rumpel S]] |
| - | [[Category: Siebel, J]] | + | [[Category: Siebel J]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q9FYU1_CHLRE
Publication Abstract from PubMed
The transfer of photosynthetic electrons by the ferredoxin PetF to the [FeFe] hydrogenase HydA1 in the microalga Chlamydomonas reinhardtii is a key step in hydrogen production. Electron delivery requires a specific interaction between PetF and HydA1. However, because of the transient nature of the electron-transfer complex, a crystal structure remains elusive. Therefore, we performed protein-protein docking based on new experimental data from a solution NMR spectroscopy investigation of native and gallium-substituted PetF. This provides valuable information about residues crucial for complex formation and electron transfer. The derived complex model might help to pinpoint residue substitution targets for improved hydrogen production.
Structural Insight into the Complex of Ferredoxin and [FeFe] Hydrogenase from Chlamydomonas reinhardtii.,Rumpel S, Siebel JF, Diallo M, Fares C, Reijerse EJ, Lubitz W Chembiochem. 2015 May 25. doi: 10.1002/cbic.201500130. PMID:26010059[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rumpel S, Siebel JF, Diallo M, Fares C, Reijerse EJ, Lubitz W. Structural Insight into the Complex of Ferredoxin and [FeFe] Hydrogenase from Chlamydomonas reinhardtii. Chembiochem. 2015 May 25. doi: 10.1002/cbic.201500130. PMID:26010059 doi:http://dx.doi.org/10.1002/cbic.201500130
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