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5Z89

Structural basis for specific inhibition of highly sensitive ShHTL7 receptor

Summary for 5Z89
Entry DOI10.2210/pdb5z89/pdb
Related5Z82
DescriptorHyposensitive to light 7, SULFATE ION, GLYCEROL, ... (5 entities in total)
Functional Keywordsstrigolactone receptor, hydrolase, striga germination signaling
Biological sourceStriga hermonthica (Purple witchweed)
Total number of polymer chains1
Total formula weight31545.25
Authors
Hameed, U.S.,Arold, S.T. (deposition date: 2018-01-31, release date: 2018-07-25, Last modification date: 2023-11-22)
Primary citationShahul Hameed, U.,Haider, I.,Jamil, M.,Kountche, B.A.,Guo, X.,Zarban, R.A.,Kim, D.,Al-Babili, S.,Arold, S.T.
Structural basis for specific inhibition of the highly sensitive ShHTL7 receptor.
EMBO Rep., 19:-, 2018
Cited by
PubMed Abstract: is a root parasitic plant that infests cereals, decimating yields, particularly in sub-Saharan Africa. For germination, seeds require host-released strigolactones that are perceived by the family of HYPOSENSITIVE to LIGHT (ShHTL) receptors. Inhibiting seed germination would thus be a promising approach for combating However, there are currently no strigolactone antagonists that specifically block ShHTLs and do not bind to DWARF14, the homologous strigolactone receptor of the host. Here, we show that the octyl phenol ethoxylate Triton X-100 inhibits seed germination without affecting host plants. High-resolution X-ray structures reveal that Triton X-100 specifically plugs the catalytic pocket of ShHTL7. ShHTL7-specific inhibition by Triton X-100 demonstrates the dominant role of this particular ShHTL receptor for germination. Our structural analysis provides a rationale for the broad specificity and high sensitivity of ShHTL7, and reveals that strigolactones trigger structural changes in ShHTL7 that are required for downstream signaling. Our findings identify Triton and the related 2-[4-(2,4,4-trimethylpentan-2-yl)phenoxy]acetic acid as promising lead compounds for the rational design of efficient -specific herbicides.
PubMed: 30021834
DOI: 10.15252/embr.201745619
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.42 Å)
Structure validation

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数据于2024-11-06公开中

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