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5GXI

Structure of the Gemin5 WD40 domain in complex with AAUUUUUGAG

5GXI の概要
エントリーDOI10.2210/pdb5gxi/pdb
関連するPDBエントリー5GXH
分子名称Gem-associated protein 5, RNA (5'-R(*A*AP*UP*UP*UP*UP*UP*GP*AP*G)-3'), UNKNOWN ATOM OR ION, ... (4 entities in total)
機能のキーワードsnrnp assembly, snrna, structural genomics, structural genomics consortium, sgc, rna binding protein-rna complex, rna binding protein/rna
由来する生物種Homo sapiens (Human)
詳細
タンパク質・核酸の鎖数2
化学式量合計87501.26
構造登録者
Xu, C.,He, H.,Li, Y.,Dong, A.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2016-09-18, 公開日: 2016-10-26, 最終更新日: 2024-10-30)
主引用文献Xu, C.,Ishikawa, H.,Izumikawa, K.,Li, L.,He, H.,Nobe, Y.,Yamauchi, Y.,Shahjee, H.M.,Wu, X.-H.,Yu, Y.-T.,Isobe, T.,Takahashi, N.,Min, J.
Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly
Genes Dev., 30:2376-2390, 2016
Cited by
PubMed Abstract: In cytoplasm, the survival of motor neuron (SMN) complex delivers pre-small nuclear RNAs (pre-snRNAs) to the heptameric Sm ring for the assembly of the ring complex on pre-snRNAs at the conserved Sm site [A(U)G]. Gemin5, a WD40 protein component of the SMN complex, is responsible for recognizing pre-snRNAs. In addition, Gemin5 has been reported to specifically bind to the mG cap. In this study, we show that the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs by isothermal titration calorimetry (ITC) and mutagenesis assays. We further determined the crystal structures of the WD40 domain of Gemin5 in complex with the Sm site or mG cap of pre-snRNA, which reveal that the WD40 domain of Gemin5 recognizes the Sm site and mG cap of pre-snRNAs via two distinct binding sites by respective base-specific interactions. In addition, we also uncovered a novel role of Gemin5 in escorting the truncated forms of U1 pre-snRNAs for proper disposal. Overall, the elucidated Gemin5 structures will contribute to a better understanding of Gemin5 in small nuclear ribonucleic protein (snRNP) biogenesis as well as, potentially, other cellular activities.
PubMed: 27881600
DOI: 10.1101/gad.288340.116
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.85 Å)
構造検証レポート
Validation report summary of 5gxi
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-29に公開中

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