3WE3

Structure of BLM RQC domain bound to an arsenate ion

3WE3 の概要

• エントリーDOI: 10.2210/pdb3we3/pdb
• 関連するPDBエントリー: 3WE2
• 分子名称: Bloom syndrome protein, ARSENATE, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: winged-helix, dna helicase, dna binding, dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P54132
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32789.40

構造登録者

Kim, S.Y.,Hakoshima, T.,Kitano, K. (登録日: 2013-06-28, 公開日: 2013-11-13, 最終更新日: 2023-11-08)

主引用文献

Kim, S.Y.,Hakoshima, T.,Kitano, K.
Structure of the RecQ C-terminal Domain of Human Bloom Syndrome Protein
Sci Rep, 3:3294-3294, 2013

PubMed Abstract: Bloom syndrome is a rare genetic disorder characterized by genomic instability and cancer predisposition. The disease is caused by mutations of the Bloom syndrome protein (BLM). Here we report the crystal structure of a RecQ C-terminal (RQC) domain from human BLM. The structure reveals three novel features of BLM RQC which distinguish it from the previous structures of the Werner syndrome protein (WRN) and RECQ1. First, BLM RQC lacks an aromatic residue at the tip of the β-wing, a key element of the RecQ-family helicases used for DNA-strand separation. Second, a BLM-specific insertion between the N-terminal helices exhibits a looping-out structure that extends at right angles to the β-wing. Deletion mutagenesis of this insertion interfered with binding to Holliday junction. Third, the C-terminal region of BLM RQC adopts an extended structure running along the domain surface, which may facilitate the spatial positioning of an HRDC domain in the full-length protein.

PubMed: 24257077
DOI: 10.1038/srep03294

実験手法

X-RAY DIFFRACTION (2.9 Å)