6AP6
Crystal Structure of DAD2 in complex with tolfenamic acid
Summary for 6AP6
| Entry DOI | 10.2210/pdb6ap6/pdb |
| Related | 4DNP |
| Descriptor | Probable strigolactone esterase DAD2, 2-[(3-chloro-2-methylphenyl)amino]benzoic acid (3 entities in total) |
| Functional Keywords | alpha/beta hydrolase, plant protein |
| Biological source | Petunia hybrida (Petunia) |
| Total number of polymer chains | 2 |
| Total formula weight | 60295.74 |
| Authors | Hamiaux, C. (deposition date: 2017-08-17, release date: 2018-03-21, Last modification date: 2023-10-04) |
| Primary citation | Hamiaux, 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: 29523686DOI: 10.1074/jbc.RA117.001154 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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