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2n0s
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(Difference between revisions)
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| - | ''' | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n0s]] is a 2 chain structure. 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> | ||
| + | </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> | ||
| + | <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'>[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://www.rcsb.org/pdb/explore.do?structureId=2n0s RCSB], [http://www.ebi.ac.uk/pdbsum/2n0s PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:26010059</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ferredoxin hydrogenase]] | ||
| + | [[Category: Fares, C]] | ||
| + | [[Category: Lubitz, W]] | ||
[[Category: Reijerse, E]] | [[Category: Reijerse, E]] | ||
[[Category: Rumpel, S]] | [[Category: Rumpel, S]] | ||
| - | [[Category: Fares, C]] | ||
[[Category: Siebel, J]] | [[Category: Siebel, J]] | ||
| - | [[Category: | + | [[Category: Oxidoreductase]] |
Revision as of 12:54, 24 June 2015
HADDOCK model of ferredoxin and [FeFe] hydrogenase complex
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