+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-43483 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
タイトル | Refined density map of gamma tubulin ring complex capped microtubule | |||||||||
マップデータ | Refined density map for gamma tubulin ring complex capped microtubule | |||||||||
試料 |
| |||||||||
キーワード | Microtubule nucleation complex bound to a microtubule / CELL CYCLE | |||||||||
機能・相同性 | 機能・相同性情報 netrin receptor binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / microtubule minus-end binding / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / equatorial microtubule organizing center / Post-chaperonin tubulin folding pathway / regulation of transepithelial transport / dorsal root ganglion development ...netrin receptor binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / microtubule minus-end binding / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / equatorial microtubule organizing center / Post-chaperonin tubulin folding pathway / regulation of transepithelial transport / dorsal root ganglion development / mitotic spindle microtubule / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / gamma-tubulin ring complex / morphogenesis of a polarized epithelium / Cilium Assembly / interphase microtubule organizing center / bBAF complex / 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 / Intraflagellar transport / GBAF complex / dense body / Formation of annular gap junctions / cytoskeleton-dependent intracellular transport / regulation of G0 to G1 transition / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / Formation of tubulin folding intermediates by CCT/TriC / microtubule nucleation / Gap junction assembly / apical protein localization / COPI-independent Golgi-to-ER retrograde traffic / regulation of double-strand break repair / 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 / Regulation of MITF-M-dependent genes involved in pigmentation / 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 / maintenance of blood-brain barrier / cortical cytoskeleton / positive regulation of stem cell population maintenance / pericentriolar material / NuA4 histone acetyltransferase complex / nitric-oxide synthase binding / cytoplasmic microtubule / cell leading edge / 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 / condensed nuclear chromosome / positive regulation of double-strand break repair via homologous recombination / mitotic spindle assembly / EPH-ephrin mediated repulsion of cells / single fertilization / 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 類似検索 - 分子機能 | |||||||||
生物種 | Homo sapiens (ヒト) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 8.5 Å | |||||||||
データ登録者 | Aher A / Urnavicius L / Kapoor TM | |||||||||
資金援助 | 米国, 1件
| |||||||||
引用 | ジャーナル: Nat Struct Mol Biol / 年: 2024 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. | |||||||||
履歴 |
|
-構造の表示
添付画像 |
---|
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_43483.map.gz | 35.7 MB | EMDBマップデータ形式 | |
---|---|---|---|---|
ヘッダ (付随情報) | emd-43483-v30.xml emd-43483.xml | 29.6 KB 29.6 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_43483_fsc.xml | 12.9 KB | 表示 | FSCデータファイル |
画像 | emd_43483.png | 117.5 KB | ||
Filedesc metadata | emd-43483.cif.gz | 10.4 KB | ||
その他 | emd_43483_half_map_1.map.gz emd_43483_half_map_2.map.gz | 140.9 MB 140.9 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-43483 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-43483 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_43483_validation.pdf.gz | 1 MB | 表示 | EMDB検証レポート |
---|---|---|---|---|
文書・詳細版 | emd_43483_full_validation.pdf.gz | 1 MB | 表示 | |
XML形式データ | emd_43483_validation.xml.gz | 20 KB | 表示 | |
CIF形式データ | emd_43483_validation.cif.gz | 26.3 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43483 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43483 | HTTPS FTP |
-関連構造データ
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
---|---|
「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_43483.map.gz / 形式: CCP4 / 大きさ: 178 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
注釈 | Refined density map for gamma tubulin ring complex capped microtubule | ||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.32 Å | ||||||||||||||||||||
密度 |
| ||||||||||||||||||||
対称性 | 空間群: 1 | ||||||||||||||||||||
詳細 | EMDB XML:
|
-添付データ
-ハーフマップ: Half map for gamma tubulin ring complex capped microtubule
ファイル | emd_43483_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
注釈 | Half map for gamma tubulin ring complex capped microtubule | ||||||||||||
投影像・断面図 |
| ||||||||||||
密度ヒストグラム |
-ハーフマップ: Half map for gamma tubulin ring complex capped microtubule
ファイル | emd_43483_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
注釈 | Half map for gamma tubulin ring complex capped microtubule | ||||||||||||
投影像・断面図 |
| ||||||||||||
密度ヒストグラム |
-試料の構成要素
+全体 : Gamma tubulin ring complex bound to microtubule minus end
+超分子 #1: Gamma tubulin ring complex bound to microtubule minus end
+分子 #1: Tubulin alpha-1B chain
+分子 #2: Tubulin beta-3 chain
+分子 #3: TUBGCP6 protein
+分子 #4: Gamma-tubulin complex component 3
+分子 #5: Mitotic-spindle organizing protein 1
+分子 #6: Actin, cytoplasmic 1
+分子 #7: Isoform 3 of Gamma-tubulin complex component 2
+分子 #8: Isoform 2 of Gamma-tubulin complex component 4
+分子 #9: Gamma-tubulin complex component 5
+分子 #10: Tubulin gamma-1 chain
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
---|---|
解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
緩衝液 | pH: 6.8 |
---|---|
凍結 | 凍結剤: ETHANE |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
---|---|
撮影 | フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 平均電子線量: 60.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 3.5 µm / 最小 デフォーカス(公称値): 1.5 µm |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |