9m74 | pdb_00009m74

Crystal structure of MBP-fused BIL1/BZR1 (21-104) in complex with double-stranded DNA contaning CACAGCTGTG

spinqualitylabelsall models 9m74, resolution 2.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9m74 is a 8 chain structure with sequence from Arabidopsis thaliana and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.23Å Ligands: EDO, GLC, PRD_900001 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A4P1LXE0_SERSF Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins.[RuleBase:RU365005]BZR1_ARATH Transcriptional repressor that binds to the brassinosteroid (BR) response element (BRRE) 5'-CGTG(T/C)G-3' in gene promoter. Regulates positively the brassinosteroid-signaling pathway (PubMed:33324437). Mediates downstream growth responses and negative feedback regulation of brassinosteroid biosynthesis. Promotes growth. Modulates ovule initiation and development by monitoring the expression of genes related to ovule development (e.g. HLL, ANT, and AP2). Negatively regulates the abscisic acid (ABA) signaling pathway during the post-germination stage (PubMed:33324437). Publication Abstract from PubMed The plant-specific transcription factor BRZ-INSENSITIVE-LONG 1 (BIL1)/BRASSINAZOLE-RESISTANT 1 (BZR1) regulates the growth of Arabidopsis thaliana via brassinosteroid signaling, acting as both a gene repressor and activator. Its upregulation requires environmental cues mediated by PHYTOCHROME INTERACTING FACTOR 4 (PIF4), with oxidative modifications via H(2)O(2) enhancing their interaction. However, the nature of the tripartite complex of cis-elements, BIL1/BZR1, and PIF4 under redox changes remains unclear. Here, we demonstrate that oxidation of the DNA-binding domain (DBD) of BIL1/BZR1 alters its DNA-binding ability. However, single cis-elements enriched in brassinosteroid-induced genes do not support binding of either redox form, nor does BIL1/BZR1 DBD heterodimerize with PIF4 DBD on these elements. These findings highlight the complexity of brassinosteroid transcriptional regulation beyond DNA-binding specificity and redox modifications. Single cis-elements in brassinosteroid-induced upregulated genes are insufficient to recruit both redox states of the BIL1/BZR1 DNA-binding domain.,Nosaki S, Ohtsuka M, Nakano T, Tanokura M, Miyakawa T FEBS Lett. 2025 Aug 29. doi: 10.1002/1873-3468.70147. PMID:40882013 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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