4ZQA

Crystal Structure of the Sds3 Dimerization Domain

4ZQA の概要

• エントリーDOI: 10.2210/pdb4zqa/pdb
• 分子名称: Sin3 histone deacetylase corepressor complex component SDS3 (2 entities in total)
• 機能のキーワード: transcription repression, histone deacetylase complex, coiled-coil, corepressor complex, transcription repressor
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10396.94

構造登録者

Chan, C.W.,Mondragon, A.,Clark, M.,Radhakrishnan, I. (登録日: 2015-05-08, 公開日: 2015-07-15, 最終更新日: 2024-03-06)

主引用文献

Clark, M.D.,Marcum, R.,Graveline, R.,Chan, C.W.,Xie, T.,Chen, Z.,Ding, Y.,Zhang, Y.,Mondragon, A.,David, G.,Radhakrishnan, I.
Structural insights into the assembly of the histone deacetylase-associated Sin3L/Rpd3L corepressor complex.
Proc.Natl.Acad.Sci.USA, 112:E3669-E3678, 2015

PubMed Abstract: Acetylation is correlated with chromatin decondensation and transcriptional activation, but its regulation by histone deacetylase (HDAC)-bearing corepressor complexes is poorly understood. Here, we describe the mechanism of assembly of the mammalian Sin3L/Rpd3L complex facilitated by Sds3, a conserved subunit deemed critical for proper assembly. Sds3 engages a globular, helical region of the HDAC interaction domain (HID) of the scaffolding protein Sin3A through a bipartite motif comprising a helix and an adjacent extended segment. Sds3 dimerizes through not only one of the predicted coiled-coil motifs but also, the segment preceding it, forming an ∼ 150-Å-long antiparallel dimer. Contrary to previous findings in yeast, Sin3A rather than Sds3 functions in recruiting HDAC1 into the complex by engaging the latter through a highly conserved segment adjacent to the helical HID subdomain. In the resulting model for the ternary complex, the two copies of the HDACs are situated distally and dynamically because of a natively unstructured linker connecting the dimerization domain and the Sin3A interaction domain of Sds3; these features contrast with the static organization described previously for the NuRD (nucleosome remodeling and deacetylase) complex. The Sds3 linker features several conserved basic residues that could potentially maintain the complex on chromatin by nonspecific interactions with DNA after initial recruitment by sequence-specific DNA-binding repressors.

PubMed: 26124119
DOI: 10.1073/pnas.1504021112

実験手法

X-RAY DIFFRACTION (1.65 Å)