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5CBK

Crystal structure of the strigolactone receptor ShHTL5 from Striga hermonthica

Summary for 5CBK
Entry DOI10.2210/pdb5cbk/pdb
DescriptorShHTL5, MAGNESIUM ION, 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL, ... (5 entities in total)
Functional Keywordsstriga hermonthica, strigolactone, signalling, receptor, shhtl5, alpha/beta hydrolase, signaling protein
Biological sourceStriga hermonthica
Total number of polymer chains1
Total formula weight31320.28
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 citationToh, 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: 26450211
DOI: 10.1126/science.aac9476
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.462 Å)
Structure validation

237735

数据于2025-06-18公开中

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