2QB0

Structure of the 2TEL crystallization module fused to T4 lysozyme with an Ala-Gly-Pro linker.

2QB0 の概要

• エントリーDOI: 10.2210/pdb2qb0/pdb
• 関連するPDBエントリー: 2QAR 2QB1
• 分子名称: Transcription factor ETV6, Transcription factor ETV6,Endolysin, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: helical polymer, hydrolase regulator
• 由来する生物種: Homo sapiens; 詳細
• 細胞内の位置: Host cytoplasm : P41212
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 74221.30

構造登録者

Nauli, S.,Bowie, J.U. (登録日: 2007-06-15, 公開日: 2008-10-14, 最終更新日: 2024-02-21)

主引用文献

Nauli, S.,Farr, S.,Lee, Y.J.,Kim, H.Y.,Faham, S.,Bowie, J.U.
Polymer-driven crystallization.
Protein Sci., 16:2542-2551, 2007

PubMed Abstract: Obtaining well-diffracting crystals of macromolecules remains a significant barrier to structure determination. Here we propose and test a new approach to crystallization, in which the crystallization target is fused to a polymerizing protein module, so that polymer formation drives crystallization of the target. We test the approach using a polymerization module called 2TEL, which consists of two tandem sterile alpha motif (SAM) domains from the protein translocation Ets leukemia (TEL). The 2TEL module is engineered to polymerize as the pH is lowered, which allows the subtle modulation of polymerization needed for crystal formation. We show that the 2TEL module can drive the crystallization of 11 soluble proteins, including three that resisted prior crystallization attempts. In addition, the 2TEL module crystallizes in the presence of various detergents, suggesting that it might facilitate membrane protein crystallization. The crystal structures of two fusion proteins show that the TELSAM polymer is responsible for the majority of contacts in the crystal lattice. The results suggest that biological polymers could be designed as crystallization modules.

PubMed: 17962407
DOI: 10.1110/ps.073074207

実験手法

X-RAY DIFFRACTION (2.56 Å)