4YHC
Crystal structure of the WD40 domain of SCAP from fission yeast
4YHC の概要
エントリーDOI | 10.2210/pdb4yhc/pdb |
分子名称 | Sterol regulatory element-binding protein cleavage-activating protein, CITRIC ACID (3 entities in total) |
機能のキーワード | beta sheet, wd40, structural protein |
由来する生物種 | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 105965.14 |
構造登録者 | |
主引用文献 | Gong, X.,Li, J.,Shao, W.,Wu, J.,Qian, H.,Ren, R.,Espenshade, P.,Yan, N. Structure of the WD40 domain of SCAP from fission yeast reveals the molecular basis for SREBP recognition. Cell Res., 25:401-411, 2015 Cited by PubMed Abstract: The sterol regulatory element-binding protein (SREBP) and SREBP cleavage-activating protein (SCAP) are central players in the SREBP pathway, which control the cellular lipid homeostasis. SCAP binds to SREBP through their carboxyl (C) domains and escorts SREBP from the endoplasmic reticulum to the Golgi upon sterol depletion. A conserved pathway, with the homologues of SREBP and SCAP being Sre1 and Scp1, was identified in fission yeast Schizosaccharomyces pombe. Here we report the in vitro reconstitution of the complex between the C domains of Sre1 and Scp1 as well as the crystal structure of the WD40 domain of Scp1 at 2.1 Å resolution. The structure reveals an eight-bladed β-propeller that exhibits several distinctive features from a canonical WD40 repeat domain. Structural and biochemical characterization led to the identification of two Scp1 elements that are involved in Sre1 recognition, an Arg/Lys-enriched surface patch on the top face of the WD40 propeller and a 30-residue C-terminal tail. The structural and biochemical findings were corroborated by in vivo examinations. These studies serve as a framework for the mechanistic understanding and further functional characterization of the SREBP and SCAP proteins in fission yeast and higher organisms. PubMed: 25771684DOI: 10.1038/cr.2015.32 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.05 Å) |
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