2N0S
HADDOCK model of ferredoxin and [FeFe] hydrogenase complex
Summary for 2N0S
| Entry DOI | 10.2210/pdb2n0s/pdb |
| NMR Information | BMRB: 19622 |
| Descriptor | Fe-hydrogenase, Ferredoxin, chloroplastic, IRON/SULFUR CLUSTER, ... (4 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Chlamydomonas reinhardtii More |
| Cellular location | Plastid, chloroplast: P07839 |
| Total number of polymer chains | 2 |
| Total formula weight | 58044.65 |
| Authors | Rumpel, S.,Siebel, J.,Fares, C.,Reijerse, E.,Lubitz, W. (deposition date: 2015-03-13, release date: 2015-06-24, Last modification date: 2024-05-15) |
| Primary citation | Rumpel, S.,Siebel, J.F.,Diallo, M.,Fares, C.,Reijerse, E.J.,Lubitz, W. Structural Insight into the Complex of Ferredoxin and [FeFe] Hydrogenase from Chlamydomonas reinhardtii. Chembiochem, 16:1663-1669, 2015 Cited by PubMed Abstract: 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. PubMed: 26010059DOI: 10.1002/cbic.201500130 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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