6RNW
The crystal structure of Thermosynechococcus elongatus protochlorophyllide oxidoreductase (POR) in complex with NADP.
Summary for 6RNW
| Entry DOI | 10.2210/pdb6rnw/pdb |
| Descriptor | NADPH-protochlorophyllide oxidoreductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | light dependent, photosynthesis |
| Biological source | Thermosynechococcus elongatus |
| Total number of polymer chains | 1 |
| Total formula weight | 39981.58 |
| Authors | Levy, C.W. (deposition date: 2019-05-09, release date: 2019-10-30, Last modification date: 2024-01-24) |
| Primary citation | Zhang, S.,Heyes, D.J.,Feng, L.,Sun, W.,Johannissen, L.O.,Liu, H.,Levy, C.W.,Li, X.,Yang, J.,Yu, X.,Lin, M.,Hardman, S.J.O.,Hoeven, R.,Sakuma, M.,Hay, S.,Leys, D.,Rao, Z.,Zhou, A.,Cheng, Q.,Scrutton, N.S. Structural basis for enzymatic photocatalysis in chlorophyll biosynthesis. Nature, 574:722-725, 2019 Cited by PubMed Abstract: The enzyme protochlorophyllide oxidoreductase (POR) catalyses a light-dependent step in chlorophyll biosynthesis that is essential to photosynthesis and, ultimately, all life on Earth. POR, which is one of three known light-dependent enzymes, catalyses reduction of the photosensitizer and substrate protochlorophyllide to form the pigment chlorophyllide. Despite its biological importance, the structural basis for POR photocatalysis has remained unknown. Here we report crystal structures of cyanobacterial PORs from Thermosynechococcus elongatus and Synechocystis sp. in their free forms, and in complex with the nicotinamide coenzyme. Our structural models and simulations of the ternary protochlorophyllide-NADPH-POR complex identify multiple interactions in the POR active site that are important for protochlorophyllide binding, photosensitization and photochemical conversion to chlorophyllide. We demonstrate the importance of active-site architecture and protochlorophyllide structure in driving POR photochemistry in experiments using POR variants and protochlorophyllide analogues. These studies reveal how the POR active site facilitates light-driven reduction of protochlorophyllide by localized hydride transfer from NADPH and long-range proton transfer along structurally defined proton-transfer pathways. PubMed: 31645759DOI: 10.1038/s41586-019-1685-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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