Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7E40

Mechanism of Phosphate Sensing and Signaling Revealed by Rice SPX1-PHR2 Complex Structure

Summary for 7E40
Entry DOI10.2210/pdb7e40/pdb
DescriptorProtein PHOSPHATE STARVATION RESPONSE 2, SPX domain-containing protein 1,Endolysin, INOSITOL HEXAKISPHOSPHATE, ... (4 entities in total)
Functional Keywordsphosphate sensing and responding, insp6-osspx1-osphr2 ternary complex, allosterically regulation, dna binding inhibition, plant protein, protein binding
Biological sourceOryza sativa subsp. japonica (Rice)
More
Total number of polymer chains4
Total formula weight114746.04
Authors
Zhou, J.,Hu, Q.,Yao, D.,Xing, W. (deposition date: 2021-02-09, release date: 2021-11-10, Last modification date: 2024-05-29)
Primary citationZhou, J.,Hu, Q.,Xiao, X.,Yao, D.,Ge, S.,Ye, J.,Li, H.,Cai, R.,Liu, R.,Meng, F.,Wang, C.,Zhu, J.K.,Lei, M.,Xing, W.
Mechanism of phosphate sensing and signaling revealed by rice SPX1-PHR2 complex structure.
Nat Commun, 12:7040-7040, 2021
Cited by
PubMed Abstract: Phosphate, a key plant nutrient, is perceived through inositol polyphosphates (InsPs) by SPX domain-containing proteins. SPX1 an inhibit the PHR2 transcription factor to maintain Pi homeostasis. How SPX1 recognizes an InsP molecule and represses transcription activation by PHR2 remains unclear. Here we show that, upon binding InsP, SPX1 can disrupt PHR2 dimers and form a 1:1 SPX1-PHR2 complex. The complex structure reveals that SPX1 helix α1 can impose a steric hindrance when interacting with the PHR2 dimer. By stabilizing helix α1, InsP allosterically decouples the PHR2 dimer and stabilizes the SPX1-PHR2 interaction. In doing so, InsP further allows SPX1 to engage with the PHR2 MYB domain and sterically block its interaction with DNA. Taken together, our results suggest that, upon sensing the surrogate signals of phosphate, SPX1 inhibits PHR2 via a dual mechanism that attenuates dimerization and DNA binding activities of PHR2.
PubMed: 34857773
DOI: 10.1038/s41467-021-27391-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

238582

数据于2025-07-09公开中

PDB statisticsPDBj update infoContact PDBjnumon