2n0s: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
m Protected "2n0s" [edit=sysop:move=sysop]
OCA (talk | contribs)
No edit summary
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 2n0s is ON HOLD
==HADDOCK model of ferredoxin and [FeFe] hydrogenase complex==
<StructureSection load='2n0s' size='340' side='right'caption='[[2n0s]]' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR,  models</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'>[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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9FYU1_CHLRE Q9FYU1_CHLRE]
<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.


Authors: Rumpel, S., Siebel, J., Fares, C., Reijerse, E., Lubitz, W.
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>


Description: HADDOCK model of ferredoxin and [FeFe] hydrogenase complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Reijerse, E]]
<div class="pdbe-citations 2n0s" style="background-color:#fffaf0;"></div>
[[Category: Rumpel, S]]
== References ==
[[Category: Fares, C]]
<references/>
[[Category: Siebel, J]]
__TOC__
[[Category: Lubitz, W]]
</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Large Structures]]
[[Category: Fares C]]
[[Category: Lubitz W]]
[[Category: Reijerse E]]
[[Category: Rumpel S]]
[[Category: Siebel J]]