3NEG
Pyrabactin-bound PYL1 structure in the open and close forms
Summary for 3NEG
| Entry DOI | 10.2210/pdb3neg/pdb |
| Related | 3KDH 3KDI 3KDJ 3NEF |
| Descriptor | Abscisic acid receptor PYL1, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide, BROMIDE ION, ... (4 entities in total) |
| Functional Keywords | pyl1, pyrabactin, hormone receptor, hydrolase |
| Biological source | Arabidopsis thaliana (mouse-ear cress) |
| Cellular location | Cytoplasm (By similarity): Q8VZS8 |
| Total number of polymer chains | 2 |
| Total formula weight | 47490.21 |
| Authors | |
| Primary citation | Hao, Q.,Yin, P.,Yan, C.,Yuan, X.,Li, W.,Zhang, Z.,Liu, L.,Wang, J.,Yan, N. Functional mechanism of the ABA agonist pyrabactin J.Biol.Chem., 285:28946-28952, 2010 Cited by PubMed Abstract: Pyrabactin is a synthetic abscisic acid (ABA) agonist that selectively inhibits seed germination. The use of pyrabactin was pivotal in the identification of the PYR1/PYL/RCAR family (PYL) of proteins as the ABA receptor. Although they both act through PYL proteins, pyrabactin and ABA share no apparent chemical or structural similarity. It remains unclear how pyrabactin functions as an ABA agonist. Here, we report the crystal structure of pyrabactin in complex with PYL1 at 2.4 A resolution. Structural and biochemical analyses revealed that recognition of pyrabactin by the pocket residues precedes the closure of switch loop CL2. Structural comparison between pyrabactin- and ABA-bound PYL1 reveals a general principle in the arrangements of function groups of the two distinct ligands. The study provides a framework for the development of novel ABA agonists that may have applicable potentials in agriculture. PubMed: 20554531DOI: 10.1074/jbc.M110.149005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.801 Å) |
Structure validation
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