6VPQ

Crystal structure of the C-terminal domain of DENR

6VPQ の概要

• エントリーDOI: 10.2210/pdb6vpq/pdb
• 分子名称: Density-regulated protein, MAGNESIUM ION, TRIETHYLENE GLYCOL, ... (6 entities in total)
• 機能のキーワード: protein synthesis regulation; translation initiation; translation reinitiation; translation recycling; density regulated protein (denr), translation
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 135348.57

構造登録者

Lomakin, I.B.,Steitz, T.A. (登録日: 2020-02-04, 公開日: 2020-04-08, 最終更新日: 2024-10-16)

主引用文献

Lomakin, I.B.,De, S.,Wang, J.,Borkar, A.N.,Steitz, T.A.
Crystal structure of the C-terminal domain of DENR.
Comput Struct Biotechnol J, 18:696-704, 2020

PubMed Abstract: The density regulated protein (DENR) forms a stable heterodimer with malignant T-cell-amplified sequence 1 (MCT-1). DENR-MCT-1 heterodimer then participates in regulation of non-canonical translation initiation and ribosomal recycling. The N-terminal domain of DENR interacts with MCT-1 and carries a classical tetrahedral zinc ion-binding site, which is crucial for the dimerization. DENR-MCT-1 binds the small (40S) ribosomal subunit through interactions between MCT-1 and helix h24 of the 18S rRNA, and through interactions between the C-terminal domain of DENR and helix h44 of the 18S rRNA. This later interaction occurs in the vicinity of the P site that is also the binding site for canonical translation initiation factor eIF1, which plays the key role in initiation codon selection and scanning. Sequence homology modeling and a low-resolution crystal structure of the DENR-MCT-1 complex with the human 40S subunit suggests that the C-terminal domain of DENR and eIF1 adopt a similar fold. Here we present the crystal structure of the C-terminal domain of DENR determined at 1.74 Å resolution, which confirms its resemblance to eIF1 and advances our understanding of the mechanism by which DENR-MCT-1 regulates non-canonical translation initiation and ribosomal recycling.

PubMed: 32257053
DOI: 10.1016/j.csbj.2020.03.009

実験手法

X-RAY DIFFRACTION (1.74 Å)