5CBK
Crystal structure of the strigolactone receptor ShHTL5 from Striga hermonthica
Summary for 5CBK
Entry DOI | 10.2210/pdb5cbk/pdb |
Descriptor | ShHTL5, MAGNESIUM ION, 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL, ... (5 entities in total) |
Functional Keywords | striga hermonthica, strigolactone, signalling, receptor, shhtl5, alpha/beta hydrolase, signaling protein |
Biological source | Striga hermonthica |
Total number of polymer chains | 1 |
Total formula weight | 31320.28 |
Authors | Stogios, P.J.,Onopriyenko, O.,Yim, V.,Savchenko, A. (deposition date: 2015-07-01, release date: 2015-10-21, Last modification date: 2023-09-27) |
Primary citation | Toh, S.,Holbrook-Smith, D.,Stogios, P.J.,Onopriyenko, O.,Lumba, S.,Tsuchiya, Y.,Savchenko, A.,McCourt, P. Structure-function analysis identifies highly sensitive strigolactone receptors in Striga. Science, 350:203-207, 2015 Cited by PubMed Abstract: Strigolactones are naturally occurring signaling molecules that affect plant development, fungi-plant interactions, and parasitic plant infestations. We characterized the function of 11 strigolactone receptors from the parasitic plant Striga hermonthica using chemical and structural biology. We found a clade of polyspecific receptors, including one that is sensitive to picomolar concentrations of strigolactone. A crystal structure of a highly sensitive strigolactone receptor from Striga revealed a larger binding pocket than that of the Arabidopsis receptor, which could explain the increased range of strigolactone sensitivity. Thus, the sensitivity of Striga to strigolactones from host plants is driven by receptor sensitivity. By expressing strigolactone receptors in Arabidopsis, we developed a bioassay that can be used to identify chemicals and crops with altered strigolactone levels. PubMed: 26450211DOI: 10.1126/science.aac9476 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.462 Å) |
Structure validation
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