2n0s | pdb_00002n0s

HADDOCK model of ferredoxin and [FeFe] hydrogenase complex

spinqualitylabelsall models 2n0s, 4 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n0s is a 2 chain structure with sequence from Chlre. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FES, SF4 Gene: hyd1, HYD1, hydA, hydA1, CHLREDRAFT_183963 (CHLRE), PETF (CHLRE) Activity: Ferredoxin hydrogenase, with EC number 1.12.7.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FER_CHLRE] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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