3NR4
Pyrabactin-bound PYL2
Summary for 3NR4
| Entry DOI | 10.2210/pdb3nr4/pdb |
| Related | 3KDH 3NEF 3NEG 3NS2 |
| Descriptor | Abscisic acid receptor PYL2, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide (3 entities in total) |
| Functional Keywords | abscisic acid signaling pathway, receptor, pyrabactin, hormone receptor |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Cytoplasm (By similarity): O80992 |
| Total number of polymer chains | 3 |
| Total formula weight | 65061.58 |
| Authors | |
| Primary citation | Yuan, X.,Yin, P.,Hao, Q.,Yan, C.,Wang, J.,Yan, N. Single amino acid alteration between Valine and Isoleucine determines the distinct pyrabactin selectivity by PYL1 and PYL2 J.Biol.Chem., 285:28953-28958, 2010 Cited by PubMed Abstract: Abscisic acid (ABA) is one of the most important phytohormones in plant. PYL proteins were identified to be ABA receptors in Arabidopsis thaliana. Despite the remarkably high degree of sequence similarity, PYL1 and PYL2 exhibit distinct responses toward pyrabactin, an ABA agonist. PYL1 inhibits protein phosphatase type 2C upon binding of pyrabactin. In contrast, PYL2 appears relatively insensitive to this compound. The crystal structure of pyrabactin-bound PYL1 revealed that most of the PYL1 residues involved in pyrabactin binding are conserved, hence failing to explain the selectivity of pyrabactin for PYL1 over PYL2. To understand the molecular basis of pyrabactin selectivity, we determined the crystal structure of PYL2 in complex with pyrabactin at 1.64 A resolution. Structural comparison and biochemical analyses demonstrated that one single amino acid alteration between a corresponding valine and isoleucine determines the distinct pyrabactin selectivity by PYL1 and PYL2. These characterizations provide an important clue to dissecting the redundancy of PYL proteins. PubMed: 20630864DOI: 10.1074/jbc.M110.160192 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.006 Å) |
Structure validation
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