4PGK
Insights into Substrate and Metal Binding from the Crystal Structure of Cyanobacterial Aldehyde Deformylating Oxygenase with Substrate Bound
Summary for 4PGK
| Entry DOI | 10.2210/pdb4pgk/pdb |
| Descriptor | Aldehyde decarbonylase, FE (III) ION, 11-[2-(2-ethoxyethoxy)ethoxy]undecanal, ... (4 entities in total) |
| Functional Keywords | non-heme di-iron protein, hydrocarbon production, alpha-helix, oxidoreductase |
| Biological source | Prochlorococcus marinus |
| Total number of polymer chains | 1 |
| Total formula weight | 27635.15 |
| Authors | Buer, B.C.,Paul, B.,Das, D.,Stuckey, J.A.,Marsh, E.N.G. (deposition date: 2014-05-02, release date: 2014-12-24, Last modification date: 2023-09-27) |
| Primary citation | Buer, B.C.,Paul, B.,Das, D.,Stuckey, J.A.,Marsh, E.N. Insights into substrate and metal binding from the crystal structure of cyanobacterial aldehyde deformylating oxygenase with substrate bound. Acs Chem.Biol., 9:2584-2593, 2014 Cited by PubMed Abstract: The nonheme diiron enzyme cyanobacterial aldehyde deformylating oxygenase, cADO, catalyzes the highly unusual deformylation of aliphatic aldehydes to alkanes and formate. We have determined crystal structures for the enzyme with a long-chain water-soluble aldehyde and medium-chain carboxylic acid bound to the active site. These structures delineate a hydrophobic channel that connects the solvent with the deeply buried active site and reveal a mode of substrate binding that is different from previously determined structures with long-chain fatty acids bound. The structures also identify a water channel leading to the active site that could facilitate the entry of protons required in the reaction. NMR studies examining 1-[(13)C]-octanal binding to cADO indicate that the enzyme binds the aldehyde form rather than the hydrated form. Lastly, the fortuitous cocrystallization of the metal-free form of the protein with aldehyde bound has revealed protein conformation changes that are involved in binding iron. PubMed: 25222710DOI: 10.1021/cb500343j PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.17 Å) |
Structure validation
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