6ELX
Oryza sativa DWARF14
Summary for 6ELX
| Entry DOI | 10.2210/pdb6elx/pdb |
| Descriptor | Strigolactone esterase D14, (4R)-2-METHYLPENTANE-2,4-DIOL, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | strigolactone, strigolactone receptor, d14, ligand binding, hydrolase |
| Biological source | Oryza sativa subsp. japonica (Rice) |
| Cellular location | Cytoplasm : Q10QA5 |
| Total number of polymer chains | 2 |
| Total formula weight | 59386.19 |
| Authors | Andersson, I.,Carlsson, G.H.,Hasse, D. (deposition date: 2017-09-29, release date: 2018-05-09, Last modification date: 2024-01-17) |
| Primary citation | Carlsson, G.H.,Hasse, D.,Cardinale, F.,Prandi, C.,Andersson, I. The elusive ligand complexes of the DWARF14 strigolactone receptor. J. Exp. Bot., 69:2345-2354, 2018 Cited by PubMed Abstract: Strigolactones, a group of terpenoid lactones, control many aspects of plant growth and development, but the active forms of these plant hormones and their mode of action at the molecular level are still unknown. The strigolactone protein receptor is unusual because it has been shown to cleave the hormone and supposedly forms a covalent bond with the cleaved hormone fragment. This interaction is suggested to induce a conformational change in the receptor that primes it for subsequent interaction with partners in the signalling pathway. Substantial efforts have been invested into describing the interaction of synthetic strigolactone analogues with the receptor, resulting in a number of crystal structures. This investigation combines a re-evaluation of models in the Protein Data Bank with a search for new conditions that may permit the capture of a receptor-ligand complex. While weak difference density is frequently observed in the binding cavity, possibly due to a low-occupancy compound, the models often contain features not supported by the X-ray data. Thus, at this stage, we do not believe that any detailed deductions about the nature, conformation, or binding mode of the ligand can be made with any confidence. PubMed: 29394369DOI: 10.1093/jxb/ery036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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