2A2F
Crystal Structure of Sec15 C-terminal domain
2A2F の概要
| エントリーDOI | 10.2210/pdb2a2f/pdb |
| 分子名称 | Exocyst complex component Sec15 (2 entities in total) |
| 機能のキーワード | all helical structure, protein transport |
| 由来する生物種 | Drosophila melanogaster (fruit fly) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 37961.69 |
| 構造登録者 | Wu, S.,Mehta, S.Q.,Pichaud, F.,Bellen, H.J.,Quiocho, F.A. (登録日: 2005-06-22, 公開日: 2005-09-13, 最終更新日: 2024-02-14) |
| 主引用文献 | Wu, S.,Mehta, S.Q.,Pichaud, F.,Bellen, H.J.,Quiocho, F.A. Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo. Nat.Struct.Mol.Biol., 12:879-885, 2005 Cited by PubMed Abstract: Sec15, a component of the exocyst, recognizes vesicle-associated Rab GTPases, helps target transport vesicles to the budding sites in yeast and is thought to recruit other exocyst proteins. Here we report the characterization of a 35-kDa fragment that comprises most of the C-terminal half of Drosophila melanogaster Sec15. This C-terminal domain was found to bind a subset of Rab GTPases, especially Rab11, in a GTP-dependent manner. We also provide evidence that in fly photoreceptors Sec15 colocalizes with Rab11 and that loss of Sec15 affects rhabdomere morphology. Determination of the 2.5-A crystal structure of the C-terminal domain revealed a novel fold consisting of ten alpha-helices equally distributed between two subdomains (N and C subdomains). We show that the C subdomain, mainly via a single helix, is sufficient for Rab binding. PubMed: 16155582DOI: 10.1038/nsmb987 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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