5LNC

Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized by carrier-driven crystallization in fusion with the macro domain of human histone macroH2A1.1

5LNC の概要

• エントリーDOI: 10.2210/pdb5lnc/pdb
• 関連するPDBエントリー: 5IIT
• 分子名称: Vacuolar transporter chaperone 4,Core histone macro-H2A.1 (1 entity in total)
• 機能のキーワード: macro domain, spx domain, inositol polyphosphate binding, carrier-driven crystallization, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• 細胞内の位置: Nucleus : O75367
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 84469.87

構造登録者

Wild, R.,Hothorn, M. (登録日: 2016-08-03, 公開日: 2016-11-09, 最終更新日: 2024-01-10)

主引用文献

Wild, R.,Hothorn, M.
The macro domain as fusion tag for carrier-driven crystallization.
Protein Sci., 26:365-374, 2017

PubMed Abstract: Obtaining well-ordered crystals remains a significant challenge in protein X-ray crystallography. Carrier-driven crystallization can facilitate crystal formation and structure solution of difficult target proteins. We obtained crystals of the small and highly flexible SPX domain from the yeast vacuolar transporter chaperone 4 (Vtc4) when fused to a C-terminal, non-cleavable macro tag derived from human histone macroH2A1.1. Initial crystals diffracted to 3.3 Å resolution. Reductive protein methylation of the fusion protein yielded a new crystal form diffracting to 2.1 Å. The structures were solved by molecular replacement, using isolated macro domain structures as search models. Our findings suggest that macro domain tags can be employed in recombinant protein expression in E. coli, and in carrier-driven crystallization.

PubMed: 27774698
DOI: 10.1002/pro.3073

実験手法

X-RAY DIFFRACTION (3.29 Å)