2HGH
Transcription Factor IIIA zinc fingers 4-6 bound to 5S rRNA 55mer (NMR structure)
2HGH の概要
| エントリーDOI | 10.2210/pdb2hgh/pdb |
| 関連するPDBエントリー | 1TF3 1ZNF |
| NMR情報 | BMRB: 7194 |
| 分子名称 | 55-MER, Transcription factor IIIA, ZINC ION (3 entities in total) |
| 機能のキーワード | zinc finger, transcription-rna complex, transcription/rna |
| 由来する生物種 | Xenopus laevis (African clawed frog) 詳細 |
| 細胞内の位置 | Nucleus: P03001 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 28122.48 |
| 構造登録者 | |
| 主引用文献 | Lee, B.M.,Xu, J.,Clarkson, B.K.,Martinez-Yamout, M.A.,Dyson, J.H.,Case, D.A.,Gottesfeld, J.M.,Wright, P.E. Induced Fit and 'Lock and Key' Recognition of 5 S RNA by Zinc Fingers of Transcription Factor IIIA J.Mol.Biol., 357:275-291, 2006 Cited by PubMed Abstract: Transcription factor IIIA (TFIIIA) is a Cys2His2 zinc finger protein that regulates expression of the 5 S ribosomal RNA gene by binding specifically to the internal control element. TFIIIA also functions in transport and storage of 5 S RNA by binding directly to the RNA transcript. To obtain insights into the mechanism by which TFIIIA recognizes 5 S RNA, we determined the solution structure of the middle three zinc fingers bound to the central core of 5 S RNA. Finger 4 utilizes "lock and key" recognition to bind in the widened major groove of the pre-structured RNA loop E motif. This interaction is mediated by direct hydrogen bonding interactions with bases. In contrast, recognition of loop A, a flexible junction of three helices, occurs by an induced fit mechanism that involves reorganization of the conserved CAUA motif and structuring of the finger 5-finger 6 interface to form a complementary RNA binding surface. PubMed: 16405997DOI: 10.1016/j.jmb.2005.12.010 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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