4RQM

Crystal structure of the SeMET BICC1 SAM Domain R924E mutant

4RQM の概要

• エントリーDOI: 10.2210/pdb4rqm/pdb
• 関連するPDBエントリー: 4RQN
• 分子名称: Protein bicaudal C homolog 1, ZINC ION (3 entities in total)
• 機能のキーワード: sam domain, protein-protein interaction domain, polymerization domain, polymerization, p-bodies, protein binding
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 24440.60

構造登録者

Leettola, C.N.,Cascio, D.,Bowie, J.U. (登録日: 2014-11-03, 公開日: 2016-01-27, 最終更新日: 2024-10-16)

主引用文献

Rothe, B.,Leettola, C.N.,Leal-Esteban, L.,Cascio, D.,Fortier, S.,Isenschmid, M.,Bowie, J.U.,Constam, D.B.
Crystal Structure of Bicc1 SAM Polymer and Mapping of Interactions between the Ciliopathy-Associated Proteins Bicc1, ANKS3, and ANKS6.
Structure, 26:209-224.e6, 2018

PubMed Abstract: Head-to-tail polymers of sterile alpha motifs (SAM) can scaffold large macromolecular complexes. Several SAM-domain proteins that bind each other are mutated in patients with cystic kidneys or laterality defects, including the Ankyrin (ANK) and SAM domain-containing proteins ANKS6 and ANKS3, and the RNA-binding protein Bicc1. To address how their interactions are regulated, we first determined a high-resolution crystal structure of a Bicc1-SAM polymer, revealing a canonical SAM polymer with a high degree of flexibility in the subunit interface orientations. We further mapped interactions between full-length and distinct domains of Bicc1, ANKS3, and ANKS6. Neither ANKS3 nor ANKS6 alone formed macroscopic homopolymers in vivo. However, ANKS3 recruited ANKS6 to Bicc1, and the three proteins together cooperatively generated giant macromolecular complexes. Thus, the giant assemblies are shaped by SAM domains, their flanking sequences, and SAM-independent protein-protein and protein-mRNA interactions.

PubMed: 29290488
DOI: 10.1016/j.str.2017.12.002

実験手法

X-RAY DIFFRACTION (1.75 Å)