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基本情報
登録情報 | データベース: PDB / ID: 8jp4 | ||||||
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タイトル | Cryo-EM structure of the head region of full-length ERGIC-53 with MCFD2 (form A) | ||||||
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機能・相同性 | ![]() Transport to the Golgi and subsequent modification / positive regulation of organelle organization / negative regulation of protein targeting to mitochondrion / Cargo concentration in the ER / RHOD GTPase cycle / endoplasmic reticulum organization / COPII-mediated vesicle transport / COPII-coated ER to Golgi transport vesicle / RHOC GTPase cycle / Golgi organization ...Transport to the Golgi and subsequent modification / positive regulation of organelle organization / negative regulation of protein targeting to mitochondrion / Cargo concentration in the ER / RHOD GTPase cycle / endoplasmic reticulum organization / COPII-mediated vesicle transport / COPII-coated ER to Golgi transport vesicle / RHOC GTPase cycle / Golgi organization / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() 類似検索 - 分子機能 | ||||||
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![]() | Watanabe, S. / Inaba, K. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structure of full-length ERGIC-53 in complex with MCFD2 for cargo transport. 著者: Satoshi Watanabe / Yoshiaki Kise / Kento Yonezawa / Mariko Inoue / Nobutaka Shimizu / Osamu Nureki / Kenji Inaba / ![]() 要旨: ERGIC-53 transports certain subsets of newly synthesized secretory proteins and membrane proteins from the endoplasmic reticulum to the Golgi apparatus. Despite numerous structural and functional ...ERGIC-53 transports certain subsets of newly synthesized secretory proteins and membrane proteins from the endoplasmic reticulum to the Golgi apparatus. Despite numerous structural and functional studies since its identification, the overall architecture and mechanism of action of ERGIC-53 remain unclear. Here we present cryo-EM structures of full-length ERGIC-53 in complex with its functional partner MCFD2. These structures reveal that ERGIC-53 exists as a homotetramer, not a homohexamer as previously suggested, and comprises a four-leaf clover-like head and a long stalk composed of three sets of four-helix coiled-coil followed by a transmembrane domain. 3D variability analysis visualizes the flexible motion of the long stalk and local plasticity of the head region. Notably, MCFD2 is shown to possess a Zn-binding site in its N-terminal lid, which appears to modulate cargo binding. Altogether, distinct mechanisms of cargo capture and release by ERGIC- 53 via the stalk bending and metal binding are proposed. | ||||||
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-関連構造データ
関連構造データ | ![]() 36467MC ![]() 8jp5C ![]() 8jp6C ![]() 8jp7C ![]() 8jp8C ![]() 8jp9C ![]() 8jpgC 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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非結晶学的対称性 (NCS) | NCSドメイン:
NCSドメイン領域: Ens-ID: ens_1
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