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基本情報
登録情報 | データベース: PDB / ID: 8vrj | ||||||
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タイトル | Rigid body fitted model for gamma tubulin ring complex capped microtubule | ||||||
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![]() | CELL CYCLE / Microtubule nucleation complex bound to a microtubule | ||||||
機能・相同性 | ![]() netrin receptor binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / equatorial microtubule organizing center / Post-chaperonin tubulin folding pathway / regulation of transepithelial transport / microtubule minus-end binding / dorsal root ganglion development ...netrin receptor binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / equatorial microtubule organizing center / Post-chaperonin tubulin folding pathway / regulation of transepithelial transport / microtubule minus-end binding / dorsal root ganglion development / morphogenesis of a polarized epithelium / mitotic spindle microtubule / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / gamma-tubulin ring complex / Cilium Assembly / bBAF complex / interphase microtubule organizing center / Carboxyterminal post-translational modifications of tubulin / polar microtubule / postsynaptic actin cytoskeleton organization / npBAF complex / gamma-tubulin complex / nBAF complex / protein localization to adherens junction / brahma complex / postsynaptic actin cytoskeleton / Tat protein binding / structural constituent of postsynaptic actin cytoskeleton / meiotic spindle organization / Sealing of the nuclear envelope (NE) by ESCRT-III / GBAF complex / Intraflagellar transport / dense body / Formation of annular gap junctions / regulation of G0 to G1 transition / cytoskeleton-dependent intracellular transport / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / Regulation of MITF-M-dependent genes involved in pigmentation / Formation of tubulin folding intermediates by CCT/TriC / microtubule nucleation / apical protein localization / Gap junction assembly / regulation of double-strand break repair / COPI-independent Golgi-to-ER retrograde traffic / adherens junction assembly / regulation of nucleotide-excision repair / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / gamma-tubulin binding / RHOF GTPase cycle / non-motile cilium / Adherens junctions interactions / Assembly and cell surface presentation of NMDA receptors / tight junction / Kinesins / Sensory processing of sound by outer hair cells of the cochlea / regulation of norepinephrine uptake / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / regulation of mitotic metaphase/anaphase transition / SWI/SNF complex / positive regulation of double-strand break repair / regulation of synaptic vesicle endocytosis / microtubule organizing center / positive regulation of T cell differentiation / apical junction complex / COPI-dependent Golgi-to-ER retrograde traffic / establishment or maintenance of cell polarity / regulation of cyclin-dependent protein serine/threonine kinase activity / intercellular bridge / cortical cytoskeleton / maintenance of blood-brain barrier / positive regulation of stem cell population maintenance / pericentriolar material / NuA4 histone acetyltransferase complex / nitric-oxide synthase binding / cell leading edge / cytoplasmic microtubule / regulation of G1/S transition of mitotic cell cycle / Recycling pathway of L1 / mitotic sister chromatid segregation / kinesin binding / brush border / calyx of Held / microtubule-based process / negative regulation of cell differentiation / RHOH GTPase cycle / mitotic spindle assembly / positive regulation of double-strand break repair via homologous recombination / single fertilization / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / spindle assembly / regulation of protein localization to plasma membrane / positive regulation of myoblast differentiation / cellular response to interleukin-4 / Hedgehog 'off' state 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: 7.7 Å | ||||||
![]() | Aher, A. / Urnavicius, L. / Kapoor, T.M. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structure of the γ-tubulin ring complex-capped microtubule. 著者: Amol Aher / Linas Urnavicius / Allen Xue / Kasahun Neselu / Tarun M Kapoor / ![]() 要旨: Microtubules are composed of α-tubulin and β-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules ...Microtubules are composed of α-tubulin and β-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules assemble with the canonical 13-protofilament architecture, resulting in micrometer-scale α/β-tubulin tracks for intracellular transport that align with, rather than spiral along, the long axis of the filament. We report that the human ~2.3 MDa γ-tubulin ring complex (γ-TuRC), an essential regulator of microtubule formation that contains 14 γ-tubulins, selectively nucleates 13-protofilament microtubules. Cryogenic electron microscopy reconstructions of γ-TuRC-capped microtubule minus ends reveal the extensive intra-domain and inter-domain motions of γ-TuRC subunits that accommodate luminal bridge components and establish lateral and longitudinal interactions between γ-tubulins and α-tubulins. Our structures suggest that γ-TuRC, an inefficient nucleation template owing to its splayed conformation, can transform into a compacted cap at the microtubule minus end and set the lattice architecture of cellular microtubules. | ||||||
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
関連構造データ | ![]() 43482MC ![]() 8vrkC ![]() 8vt7C M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 ( |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
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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 , 8種, 53分子 1OPQRSTUVWXYZ2opqrstuvwxyz36L7...
#1: タンパク質 | 分子量: 51019.297 Da / 分子数: 13 / 変異: E254D / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() 参照: UniProt: P68363, 加水分解酵素; 酸無水物に作用; GTP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: 51276.367 Da / 分子数: 13 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #3: タンパク質 | 分子量: 199732.516 Da / 分子数: 3 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #5: タンパク質 | 分子量: 8485.724 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #6: 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) ![]() ![]() #7: タンパク質 | 分子量: 105581.500 Da / 分子数: 5 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #8: タンパク質 | 分子量: 76108.898 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #10: タンパク質 | 分子量: 52022.617 Da / 分子数: 14 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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-Gamma-tubulin complex component ... , 2種, 7分子 5BDFHNJ
#4: タンパク質 | 分子量: 103710.102 Da / 分子数: 6 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #9: タンパク質 | | 分子量: 118367.406 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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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 | 名称: Gamma tubulin ring complex bound to microtubule minus end タイプ: COMPLEX / Entity ID: all / 由来: RECOMBINANT |
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由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() |
緩衝液 | pH: 6.8 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
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: BRIGHT FIELD / 最大 デフォーカス(公称値): 3500 nm / 最小 デフォーカス(公称値): 1500 nm |
撮影 | 電子線照射量: 60 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
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解析
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3次元再構成 | 解像度: 7.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 32375 / 対称性のタイプ: POINT |
原子モデル構築 | プロトコル: RIGID BODY FIT |