5zd4 | pdb_00005zd4
Crystal structure of MBP-fused BIL1/BZR1 in complex with double-stranded DNA
Structural highlights
FunctionMALE_ECO57 Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).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). Regulates negatively the abscisic acid (ABA) signaling pathway during the post-germination stage (PubMed:33324437).[1] [2] [3] Publication Abstract from PubMedBRZ-INSENSITIVE-LONG HYPOCOTYL 1 (BIL1)/BRASSINAZOLE-RESISTANT 1 (BZR1) is a master transcription factor of brassinosteroid (BR) signalling. The varieties of nucleobase recognition of the NN-BRRE-core motif (NNCGTG), one of variant G-box motifs, distinguish BIL1/BZR1 from basic helix-loop-helix transcription factors, underlying the specific regulation of BR-responsive genes. Here, we show the non-canonical bHLH dimer formation of BIL1/BZR1 to optimize the interaction network with DNA and the orientation of a key residue for NN-BRRE-core motif recognition. Structural basis for brassinosteroid response by BIL1/BZR1.,Nosaki S, Miyakawa T, Xu Y, Nakamura A, Hirabayashi K, Asami T, Nakano T, Tanokura M Nat Plants. 2018 Oct;4(10):771-776. doi: 10.1038/s41477-018-0255-1. Epub 2018 Oct, 1. PMID:30287951[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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