+
データを開く
-
基本情報
登録情報 | データベース: PDB / ID: 6lth | ||||||
---|---|---|---|---|---|---|---|
タイトル | Structure of human BAF Base module | ||||||
![]() |
| ||||||
![]() | GENE REGULATION / Chromatin remodeler / Complex | ||||||
機能・相同性 | ![]() negative regulation of myeloid progenitor cell differentiation / single stranded viral RNA replication via double stranded DNA intermediate / histone H3K14ac reader activity / positive regulation of glucose mediated signaling pathway / histone H4K16ac reader activity / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / bBAF complex / negative regulation of androgen receptor signaling pathway / npBAF complex / nBAF complex ...negative regulation of myeloid progenitor cell differentiation / single stranded viral RNA replication via double stranded DNA intermediate / histone H3K14ac reader activity / positive regulation of glucose mediated signaling pathway / histone H4K16ac reader activity / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / bBAF complex / negative regulation of androgen receptor signaling pathway / npBAF complex / nBAF complex / brahma complex / neural retina development / blastocyst hatching / N-acetyltransferase activity / GBAF complex / EGR2 and SOX10-mediated initiation of Schwann cell myelination / histone H3K9me2/3 reader activity / nucleosome array spacer activity / regulation of G0 to G1 transition / Tat protein binding / hepatocyte differentiation / XY body / RSC-type complex / regulation of nucleotide-excision repair / RNA polymerase I preinitiation complex assembly / ATP-dependent chromatin remodeler activity / host-mediated activation of viral transcription / nucleosome disassembly / germ cell nucleus / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / cellular response to fatty acid / positive regulation of T cell differentiation / nuclear androgen receptor binding / positive regulation of double-strand break repair / nuclear chromosome / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / positive regulation of stem cell population maintenance / Regulation of MITF-M-dependent genes involved in pigmentation / regulation of G1/S transition of mitotic cell cycle / positive regulation of signal transduction by p53 class mediator / negative regulation of cell differentiation / positive regulation of Wnt signaling pathway / ATP-dependent activity, acting on DNA / positive regulation of myoblast differentiation / Chromatin modifying enzymes / DNA polymerase binding / neurogenesis / positive regulation of DNA-binding transcription factor activity / Interleukin-7 signaling / transcription initiation-coupled chromatin remodeling / transcription coregulator binding / : / nuclear receptor binding / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / positive regulation of cell differentiation / transcription coregulator activity / apoptotic signaling pathway / helicase activity / Formation of the beta-catenin:TCF transactivating complex / negative regulation of cell growth / kinetochore / DNA integration / 加水分解酵素; 酸無水物に作用; 酸無水物に作用・細胞または細胞小器官の運動に関与 / positive regulation of miRNA transcription / RMTs methylate histone arginines / nuclear matrix / fibrillar center / transcription corepressor activity / p53 binding / nervous system development / positive regulation of cold-induced thermogenesis / molecular adaptor activity / histone binding / transcription coactivator activity / hydrolase activity / chromatin remodeling / signaling receptor binding / negative regulation of cell population proliferation / negative regulation of DNA-templated transcription / intracellular membrane-bounded organelle / apoptotic process / positive regulation of cell population proliferation / centrosome / chromatin binding / regulation of transcription by RNA polymerase II / chromatin / positive regulation of DNA-templated transcription / nucleolus / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / extracellular space / RNA binding / zinc ion binding / nucleoplasm / ATP binding / identical protein binding / nucleus 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3 Å | ||||||
![]() | He, S. / Wu, Z. / Tian, Y. / Yu, Z. / Yu, J. / Wang, X. / Li, J. / Liu, B. / Xu, Y. | ||||||
![]() | ![]() タイトル: Structure of nucleosome-bound human BAF complex. 著者: Shuang He / Zihan Wu / Yuan Tian / Zishuo Yu / Jiali Yu / Xinxin Wang / Jie Li / Bijun Liu / Yanhui Xu / ![]() 要旨: Mammalian SWI/SNF family chromatin remodelers, BRG1/BRM-associated factor (BAF) and polybromo-associated BAF (PBAF), regulate chromatin structure and transcription, and their mutations are linked to ...Mammalian SWI/SNF family chromatin remodelers, BRG1/BRM-associated factor (BAF) and polybromo-associated BAF (PBAF), regulate chromatin structure and transcription, and their mutations are linked to cancers. The 3.7-angstrom-resolution cryo-electron microscopy structure of human BAF bound to the nucleosome reveals that the nucleosome is sandwiched by the base and the adenosine triphosphatase (ATPase) modules, which are bridged by the actin-related protein (ARP) module. The ATPase motor is positioned proximal to nucleosomal DNA and, upon ATP hydrolysis, engages with and pumps DNA along the nucleosome. The C-terminal α helix of SMARCB1, enriched in positively charged residues frequently mutated in cancers, mediates interactions with an acidic patch of the nucleosome. AT-rich interactive domain-containing protein 1A (ARID1A) and the SWI/SNF complex subunit SMARCC serve as a structural core and scaffold in the base module organization, respectively. Our study provides structural insights into subunit organization and nucleosome recognition of human BAF complex. | ||||||
履歴 |
|
-
構造の表示
ムービー |
![]() |
---|---|
構造ビューア | 分子: ![]() ![]() |
-
ダウンロードとリンク
-
ダウンロード
PDBx/mmCIF形式 | ![]() | 459.5 KB | 表示 | ![]() |
---|---|---|---|---|
PDB形式 | ![]() | 299.6 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 750.6 KB | 表示 | ![]() |
---|---|---|---|---|
文書・詳細版 | ![]() | 780.8 KB | 表示 | |
XML形式データ | ![]() | 56 KB | 表示 | |
CIF形式データ | ![]() | 83.3 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
-
リンク
-
集合体
登録構造単位 | ![]()
|
---|---|
1 |
|
-
要素
-タンパク質 , 4種, 5分子 ILNOR
#1: タンパク質 | 分子量: 184923.828 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() 参照: UniProt: P51532, 加水分解酵素; 酸無水物に作用; 酸無水物に作用・細胞または細胞小器官の運動に関与 | ||
---|---|---|---|
#2: タンパク質 | 分子量: 242250.312 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() | ||
#4: タンパク質 | 分子量: 133048.109 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #7: タンパク質 | | 分子量: 44222.547 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
-SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily ... , 3種, 3分子 MPQ
#3: タンパク質 | 分子量: 44199.188 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
---|---|
#5: タンパク質 | 分子量: 58311.391 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
#6: タンパク質 | 分子量: 46710.371 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
-非ポリマー , 1種, 1分子 
#8: 化合物 | ChemComp-ZN / |
---|
-詳細
研究の焦点であるリガンドがあるか | Y |
---|
-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
---|---|
EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
-
試料調製
構成要素 | 名称: Structure of human BAF Base module / タイプ: COMPLEX / Entity ID: #1-#7 / 由来: RECOMBINANT |
---|---|
分子量 | 単位: KILODALTONS/NANOMETER / 実験値: NO |
由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() |
緩衝液 | pH: 8 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | グリッドの材料: GOLD / グリッドのサイズ: 300 divisions/in. / グリッドのタイプ: Quantifoil R1.2/1.3 |
急速凍結 | 凍結剤: ETHANE / 湿度: 100 % |
-
電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
---|---|
顕微鏡 | モデル: FEI TITAN KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: OTHER |
試料ホルダ | 凍結剤: NITROGEN |
撮影 | 電子線照射量: 50 e/Å2 / 検出モード: SUPER-RESOLUTION フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
電子光学装置 | エネルギーフィルタースリット幅: 20 eV |
画像スキャン | 動画フレーム数/画像: 32 / 利用したフレーム数/画像: 1-32 |
-
解析
ソフトウェア | 名称: PHENIX / バージョン: 1.16_3549: / 分類: 精密化 | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
EMソフトウェア |
| ||||||||||||||||||||||||||||||||||||
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
対称性 | 点対称性: C1 (非対称) | ||||||||||||||||||||||||||||||||||||
3次元再構成 | 解像度: 3 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 197606 / 対称性のタイプ: POINT | ||||||||||||||||||||||||||||||||||||
原子モデル構築 | プロトコル: AB INITIO MODEL / 空間: REAL | ||||||||||||||||||||||||||||||||||||
拘束条件 |
|