3KDJ
Complex structure of (+)-ABA-bound PYL1 and ABI1
Summary for 3KDJ
Entry DOI | 10.2210/pdb3kdj/pdb |
Related | 3kdh 3kdi |
Descriptor | Putative uncharacterized protein At5g46790, Protein phosphatase 2C 56, (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid, ... (5 entities in total) |
Functional Keywords | aba, pyl1, abi1, abscisic acid signaling pathway, cell membrane, hydrolase, magnesium, manganese, metal-binding, nucleus, protein phosphatase, hydrolase-hormone receptor complex, hydrolase/hormone receptor |
Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
Cellular location | Cytoplasm (By similarity): Q8VZS8 Nucleus: P49597 |
Total number of polymer chains | 2 |
Total formula weight | 58439.99 |
Authors | |
Primary citation | Yin, P.,Fan, H.,Hao, Q.,Yuan, X.,Wu, D.,Pang, Y.,Yan, C.,Li, W.,Wang, J.,Yan, N. Structural insights into the mechanism of abscisic acid signaling by PYL proteins Nat.Struct.Mol.Biol., 16:1230-1236, 2009 Cited by PubMed Abstract: Abscisic acid (ABA) is an important phytohormone that regulates plant stress responses. Proteins from the PYR-PYL-RCAR family were recently identified as ABA receptors. Upon binding to ABA, a PYL protein associates with type 2C protein phosphatases (PP2Cs) such as ABI1 and ABI2, inhibiting their activity; the molecular mechanisms by which PYLs mediate ABA signaling remain unknown, however. Here we report three crystal structures: apo-PYL2, (+)-ABA-bound PYL2 and (+)-ABA-bound PYL1 in complex with phosphatase ABI1. Apo-PYL2 contains a pocket surrounded by four highly conserved surface loops. In response to ABA binding, loop CL2 closes onto the pocket, creating a surface that recognizes ABI1. In the ternary complex, the CL2 loop is located near the active site of ABI1, blocking the entry of substrate proteins. Together, our data reveal the mechanisms by which ABA regulates PYL-mediated inhibition of PP2Cs. PubMed: 19893533DOI: 10.1038/nsmb.1730 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.878 Å) |
Structure validation
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