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基本情報
登録情報 | データベース: PDB / ID: 6ltj | ||||||
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タイトル | Structure of nucleosome-bound human BAF complex | ||||||
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![]() | 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 / positive regulation of norepinephrine uptake / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / histone H4K16ac reader activity / cellular response to cytochalasin B / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I ...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 / positive regulation of norepinephrine uptake / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / histone H4K16ac reader activity / cellular response to cytochalasin B / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / negative regulation of androgen receptor signaling pathway / bBAF complex / npBAF complex / regulation of transepithelial transport / histone H3K9me2/3 reader activity / nBAF complex / brahma complex / morphogenesis of a polarized epithelium / blastocyst hatching / neural retina development / protein localization to adherens junction / postsynaptic actin cytoskeleton / structural constituent of postsynaptic actin cytoskeleton / N-acetyltransferase activity / Formation of the dystrophin-glycoprotein complex (DGC) / GBAF complex / Formation of annular gap junctions / EGR2 and SOX10-mediated initiation of Schwann cell myelination / Tat protein binding / nucleosome array spacer activity / Gap junction degradation / regulation of G0 to G1 transition / Folding of actin by CCT/TriC / Cell-extracellular matrix interactions / dense body / hepatocyte differentiation / XY body / Ino80 complex / regulation of nucleotide-excision repair / Prefoldin mediated transfer of substrate to CCT/TriC / ATP-dependent chromatin remodeler activity / RSC-type complex / apical protein localization / regulation of double-strand break repair / blastocyst formation / RNA polymerase I preinitiation complex assembly / adherens junction assembly / RHOF GTPase cycle / Adherens junctions interactions / positive regulation by host of viral transcription / tight junction / nucleosome disassembly / Sensory processing of sound by outer hair cells of the cochlea / germ cell nucleus / Interaction between L1 and Ankyrins / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / Sensory processing of sound by inner hair cells of the cochlea / positive regulation of T cell differentiation / cellular response to fatty acid / regulation of norepinephrine uptake / transporter regulator activity / apical junction complex / nuclear androgen receptor binding / nitric-oxide synthase binding / positive regulation of double-strand break repair / nuclear chromosome / spinal cord development / maintenance of blood-brain barrier / regulation of chromosome organization / NuA4 histone acetyltransferase complex / establishment or maintenance of cell polarity / cortical cytoskeleton / 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 / Recycling pathway of L1 / regulation of synaptic vesicle endocytosis / regulation of G1/S transition of mitotic cell cycle / regulation of DNA replication / brush border / regulation of embryonic development / kinesin binding / EPH-ephrin mediated repulsion of cells / negative regulation of cell differentiation / positive regulation of Wnt signaling pathway / ATP-dependent activity, acting on DNA / RHO GTPases Activate WASPs and WAVEs / positive regulation of myoblast differentiation / RHO GTPases activate IQGAPs / positive regulation of double-strand break repair via homologous recombination / regulation of DNA repair / regulation of protein localization to plasma membrane / Chromatin modifying enzymes / DNA polymerase binding / neurogenesis / cytoskeleton organization / EPHB-mediated forward signaling / substantia nigra development / calyx of Held 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: 3.7 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. | ||||||
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ムービー |
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構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 865.7 KB | 表示 | ![]() |
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アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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リンク
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集合体
登録構造単位 | ![]()
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要素
-タンパク質 , 10種, 15分子 AEBFCGDHIJKLNOR
#1: タンパク質 | 分子量: 15360.983 Da / 分子数: 2 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 発現宿主: ![]() ![]() #2: タンパク質 | 分子量: 11394.426 Da / 分子数: 2 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 発現宿主: ![]() ![]() #3: タンパク質 | 分子量: 13993.295 Da / 分子数: 2 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 発現宿主: ![]() ![]() #4: タンパク質 | 分子量: 13873.086 Da / 分子数: 2 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 遺伝子: H2B / 発現宿主: ![]() ![]() #5: 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 #6: タンパク質 | | 分子量: 45236.273 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #7: タンパク質 | | 分子量: 41782.660 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #8: タンパク質 | | 分子量: 142316.531 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #10: 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) ![]() ![]() #13: タンパク質 | | 分子量: 32781.926 Da / 分子数: 1 / Fragment: UNP residues 1-100, UNP residues 209-391 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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-SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily ... , 3種, 3分子 MPQ
#9: タンパク質 | 分子量: 38015.094 Da / 分子数: 1 / Fragment: UNP residues 1-113, UNP residues 172-385 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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#11: 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) ![]() ![]() |
#12: 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) ![]() ![]() |
-DNA鎖 , 2種, 2分子 XY
#14: DNA鎖 | 分子量: 36520.266 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) ![]() |
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#15: DNA鎖 | 分子量: 36929.520 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) ![]() |
-非ポリマー , 1種, 1分子 
#16: 化合物 | ChemComp-ZN / |
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-詳細
研究の焦点であるリガンドがあるか | Y |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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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 |
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試料調製
構成要素 |
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分子量 | 単位: KILODALTONS/NANOMETER / 実験値: NO | ||||||||||||||||||||||||
由来(天然) |
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由来(組換発現) |
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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 % |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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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 |
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) |
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解析
EMソフトウェア | 名称: RELION / バージョン: 3.0.8 / カテゴリ: 3次元再構成 |
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CTF補正 | タイプ: NONE |
対称性 | 点対称性: C1 (非対称) |
3次元再構成 | 解像度: 3.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 320658 / 対称性のタイプ: POINT |