1D3W
Crystal structure of ferredoxin 1 d15e mutant from azotobacter vinelandii at 1.7 angstrom resolution.
Summary for 1D3W
| Entry DOI | 10.2210/pdb1d3w/pdb |
| Related | 1BOT 1FDD 6FDR 7FDR |
| Descriptor | FERREDOXIN 1, IRON/SULFUR CLUSTER, FE3-S4 CLUSTER, ... (4 entities in total) |
| Functional Keywords | beta sheet, protein monomer, iron-sulphur protein, ferredoxin, electron transport |
| Biological source | Azotobacter vinelandii |
| Total number of polymer chains | 1 |
| Total formula weight | 12720.99 |
| Authors | Chen, K.,Hirst, J.,Camba, R.,Bonagura, C.A.,Stout, C.D.,Burges, B.K.,Armstrong, F.A. (deposition date: 1999-10-01, release date: 1999-10-14, Last modification date: 2024-02-07) |
| Primary citation | Chen, K.,Hirst, J.,Camba, R.,Bonagura, C.A.,Stout, C.D.,Burgess, B.K.,Armstrong, F.A. Atomically defined mechanism for proton transfer to a buried redox centre in a protein. Nature, 405:814-817, 2000 Cited by PubMed Abstract: The basis of the chemiosmotic theory is that energy from light or respiration is used to generate a trans-membrane proton gradient. This is largely achieved by membrane-spanning enzymes known as 'proton pumps. There is intense interest in experiments which reveal, at the molecular level, how protons are drawn through proteins. Here we report the mechanism, at atomic resolution, for a single long-range electron-coupled proton transfer. In Azotobacter vinelandii ferredoxin I, reduction of a buried iron-sulphur cluster draws in a solvent proton, whereas re-oxidation is 'gated' by proton release to the solvent. Studies of this 'proton-transferring module' by fast-scan protein film voltammetry, high-resolution crystallography, site-directed mutagenesis and molecular dynamics, reveal that proton transfer is exquisitely sensitive to the position and pK of a single amino acid. The proton is delivered through the protein matrix by rapid penetrative excursions of the side-chain carboxylate of a surface residue (Asp 15), whose pK shifts in response to the electrostatic charge on the iron-sulphur cluster. Our analysis defines the structural, dynamic and energetic requirements for proton courier groups in redox-driven proton-pumping enzymes. PubMed: 10866206DOI: 10.1038/35015610 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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