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

8E3R

Human PU.1 ETS-Domain (165-270) Bound to d(AATAAAAGGAAGTGGG)

Summary for 8E3R
Entry DOI10.2210/pdb8e3r/pdb
Related8E3K
DescriptorDNA (5'-D(*AP*AP*TP*AP*AP*AP*AP*GP*GP*AP*AP*GP*TP*GP*GP*G)-3'), DNA (5'-D(*TP*CP*CP*CP*AP*CP*TP*TP*CP*CP*TP*TP*TP*TP*AP*T)-3'), Transcription factor PU.1, ... (4 entities in total)
Functional Keywordstranscription factor, protein-dna complex, ets family, ets, pu.1, transcription-dna complex, transcription/dna
Biological sourceHomo sapiens (human)
More
Total number of polymer chains3
Total formula weight22230.99
Authors
Terrell, J.R.,Poon, G.M.K. (deposition date: 2022-08-17, release date: 2023-07-05, Last modification date: 2023-10-25)
Primary citationTerrell, J.R.,Taylor, S.J.,Schneider, A.L.,Lu, Y.,Vernon, T.N.,Xhani, S.,Gumpper, R.H.,Luo, M.,Wilson, W.D.,Steidl, U.,Poon, G.M.K.
DNA selection by the master transcription factor PU.1.
Cell Rep, 42:112671-112671, 2023
Cited by
PubMed Abstract: The master transcriptional regulator PU.1/Spi-1 engages DNA sites with affinities spanning multiple orders of magnitude. To elucidate this remarkable plasticity, we have characterized 22 high-resolution co-crystallographic PU.1/DNA complexes across the addressable affinity range in myeloid gene transactivation. Over a purine-rich core (such as 5'-GGAA-3') flanked by variable sequences, affinity is negotiated by direct readout on the 5' flank via a critical glutamine (Q226) sidechain and by indirect readout on the 3' flank by sequence-dependent helical flexibility. Direct readout by Q226 dynamically specifies PU.1's characteristic preference for purines and explains the pathogenic mutation Q226E in Waldenström macroglobulinemia. The structures also reveal how disruption of Q226 mediates strand-specific inhibition by DNA methylation and the recognition of non-canonical sites, including the authentic binding sequence at the CD11b promoter. A re-synthesis of phylogenetic and structural data on the ETS family, considering the centrality of Q226 in PU.1, unifies the model of DNA selection by ETS proteins.
PubMed: 37352101
DOI: 10.1016/j.celrep.2023.112671
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

227561

건을2024-11-20부터공개중

PDB statisticsPDBj update infoContact PDBjnumon