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2n0s

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'''Unreleased structure'''
 
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The entry 2n0s is ON HOLD
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==HADDOCK model of ferredoxin and [FeFe] hydrogenase complex==
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<StructureSection load='2n0s' size='340' side='right'caption='[[2n0s]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9FYU1_CHLRE Q9FYU1_CHLRE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Rumpel, S., Siebel, J., Fares, C., Reijerse, E., Lubitz, W.
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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>
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Description: HADDOCK model of ferredoxin and [FeFe] hydrogenase complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Reijerse, E]]
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<div class="pdbe-citations 2n0s" style="background-color:#fffaf0;"></div>
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[[Category: Rumpel, S]]
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== References ==
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[[Category: Fares, C]]
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<references/>
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[[Category: Siebel, J]]
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__TOC__
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[[Category: Lubitz, W]]
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</StructureSection>
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[[Category: Chlamydomonas reinhardtii]]
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[[Category: Large Structures]]
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[[Category: Fares C]]
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[[Category: Lubitz W]]
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[[Category: Reijerse E]]
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[[Category: Rumpel S]]
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[[Category: Siebel J]]

Current revision

HADDOCK model of ferredoxin and [FeFe] hydrogenase complex

PDB ID 2n0s

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