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6AP8

Crystal Structure of rice D14 bound to 2-(2-methyl-3-nitroanilino)benzoic acid

Summary for 6AP8
Entry DOI10.2210/pdb6ap8/pdb
Related3W04
DescriptorStrigolactone esterase D14, 2-[(2-methyl-3-nitrophenyl)amino]benzoic acid, GLYCEROL, ... (4 entities in total)
Functional Keywordsalpha/beta hydrolase, plant protein
Biological sourceOryza sativa subsp. japonica (Rice)
Cellular locationCytoplasm : Q10QA5
Total number of polymer chains2
Total formula weight59462.09
Authors
Hamiaux, C. (deposition date: 2017-08-17, release date: 2018-03-21, Last modification date: 2023-10-04)
Primary citationHamiaux, C.,Drummond, R.S.M.,Luo, Z.,Lee, H.W.,Sharma, P.,Janssen, B.J.,Perry, N.B.,Denny, W.A.,Snowden, K.C.
Inhibition of strigolactone receptors byN-phenylanthranilic acid derivatives: Structural and functional insights.
J. Biol. Chem., 293:6530-6543, 2018
Cited by
PubMed Abstract: The strigolactone (SL) family of plant hormones regulates a broad range of physiological processes affecting plant growth and development and also plays essential roles in controlling interactions with parasitic weeds and symbiotic fungi. Recent progress elucidating details of SL biosynthesis, signaling, and transport offers many opportunities for discovering new plant-growth regulators via chemical interference. Here, using high-throughput screening and downstream biochemical assays, we identified -phenylanthranilic acid derivatives as potent inhibitors of the SL receptors from petunia (DAD2), rice (OsD14), and (AtD14). Crystal structures of DAD2 and OsD14 in complex with inhibitors further provided detailed insights into the inhibition mechanism, and modeling of 19 other plant strigolactone receptors suggested that these compounds are active across a large range of plant species. Altogether, these results provide chemical tools for investigating SL signaling and further define a framework for structure-based approaches to design and validate optimized inhibitors of SL receptors for specific plant targets.
PubMed: 29523686
DOI: 10.1074/jbc.RA117.001154
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.27 Å)
Structure validation

238582

數據於2025-07-09公開中

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