3ZV0
Structure of the SHQ1P-CBF5P complex
3ZV0 の概要
| エントリーDOI | 10.2210/pdb3zv0/pdb |
| 関連するPDBエントリー | 3ZUZ |
| 分子名称 | PROTEIN SHQ1, H/ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT 4, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | cell cycle, rnp assembly, x-linked dyskeratosis congenita, telomerase |
| 由来する生物種 | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 131170.46 |
| 構造登録者 | Walbott, H.,Machado-Pinilla, R.,Liger, D.,Blaud, M.,Rety, S.,Grozdanov, P.N.,Godin, K.,vanTilbeurgh, H.,Varani, G.,Meier, U.T.,Leulliot, N. (登録日: 2011-07-22, 公開日: 2011-11-30, 最終更新日: 2024-05-08) |
| 主引用文献 | Walbott, H.,Machado-Pinilla, R.,Liger, D.,Blaud, M.,Rety, S.,Grozdanov, P.N.,Godin, K.,Van Tilbeurgh, H.,Varani, G.,Meier, U.T.,Leulliot, N. The H/Aca Rnp Assembly Factor Shq1 Functions as an RNA Mimic. Genes Dev., 25:2398-, 2011 Cited by PubMed Abstract: SHQ1 is an essential assembly factor for H/ACA ribonucleoproteins (RNPs) required for ribosome biogenesis, pre-mRNA splicing, and telomere maintenance. SHQ1 binds dyskerin/NAP57, the catalytic subunit of human H/ACA RNPs, and this interaction is modulated by mutations causing X-linked dyskeratosis congenita. We report the crystal structure of the C-terminal domain of yeast SHQ1, Shq1p, and its complex with yeast dyskerin/NAP57, Cbf5p, lacking its catalytic domain. The C-terminal domain of Shq1p interacts with the RNA-binding domain of Cbf5p and, through structural mimicry, uses the RNA-protein-binding sites to achieve a specific protein-protein interface. We propose that Shq1p operates as a Cbf5p chaperone during RNP assembly by acting as an RNA placeholder, thereby preventing Cbf5p from nonspecific RNA binding before association with an H/ACA RNA and the other core RNP proteins. PubMed: 22085966DOI: 10.1101/GAD.176834.111 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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