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3KDJ

Complex structure of (+)-ABA-bound PYL1 and ABI1

Summary for 3KDJ
Entry DOI10.2210/pdb3kdj/pdb
Related3kdh 3kdi
DescriptorPutative 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 Keywordsaba, pyl1, abi1, abscisic acid signaling pathway, cell membrane, hydrolase, magnesium, manganese, metal-binding, nucleus, protein phosphatase, hydrolase-hormone receptor complex, hydrolase/hormone receptor
Biological sourceArabidopsis thaliana (Mouse-ear cress)
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Cellular locationCytoplasm (By similarity): Q8VZS8
Nucleus: P49597
Total number of polymer chains2
Total formula weight58439.99
Authors
Yin, P.,Fan, H.,Hao, Q.,Yuan, X.,Yan, N. (deposition date: 2009-10-23, release date: 2009-11-10, Last modification date: 2023-11-01)
Primary citationYin, 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: 19893533
DOI: 10.1038/nsmb.1730
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.878 Å)
Structure validation

226707

数据于2024-10-30公开中

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