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3NR4

Pyrabactin-bound PYL2

Summary for 3NR4
Entry DOI10.2210/pdb3nr4/pdb
Related3KDH 3NEF 3NEG 3NS2
DescriptorAbscisic acid receptor PYL2, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide (3 entities in total)
Functional Keywordsabscisic acid signaling pathway, receptor, pyrabactin, hormone receptor
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Cellular locationCytoplasm (By similarity): O80992
Total number of polymer chains3
Total formula weight65061.58
Authors
Yan, N. (deposition date: 2010-06-30, release date: 2010-07-14, Last modification date: 2023-11-01)
Primary citationYuan, 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: 20630864
DOI: 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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