title: Crystal structures of the Arabidopsis thaliana abscisic acid receptor PYL10 and its complex with abscisic acid.
abstract: Abscisic acid (ABA) is one of the most essential phytohormones, and plays an important role in growth and development regulation, as well as in stress responses. The PYR/PYL/RCAR family (PYL for short)-comprised of 14 proteins in Arabidopsis-was recently identified as soluble ABA receptors that function in the perception and transduction of ABA signaling. In this work, the crystal structures of PYL10 were determined in the apo- and ABA-bound states, with respective resolutions of 3.0 and 2.7Å. Surprisingly, a closed CL2 conformation was observed in the apo-PYL10 structure, which was different from a previously reported open CL2 conformation. A putative two-conformation dynamical equilibrium model was proposed to explain PYL10's constitutive binding to PP2Cs in the apo-state and its increased PP2C binding ability in the ABA-bound state.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
authors.forename: Demeng
authors.initials: D
authors.lastname: Sun
authors.forename: Haipeng
authors.initials: H
authors.lastname: Wang
authors.forename: Minhao
authors.initials: M
authors.lastname: Wu
authors.forename: Jianye
authors.initials: J
authors.lastname: Zang
authors.forename: Fangming
authors.initials: F
authors.lastname: Wu
authors.forename: Changlin
authors.initials: C
authors.lastname: Tian
mesh_terms: D000040:Abscisic Acid / Q000737:chemistry*; D017360:Arabidopsis / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D017433:Protein Structure, Secondary; D011956:Receptors, Cell Surface / Q000737:chemistry*
chemical_list: D029681:Arabidopsis Proteins; C560427:PYL10 protein, Arabidopsis; D011956:Receptors, Cell Surface; D000040:Abscisic Acid