6T58

Structure determination of the transactivation domain of p53 in complex with S100A4 using annexin A2 as a crystallization chaperone

6T58 の概要

• エントリーDOI: 10.2210/pdb6t58/pdb
• 分子名称: Cellular tumor antigen p53,Protein S100-A4,Protein S100-A4,Annexin A2, GLYCEROL, CALCIUM ION (3 entities in total)
• 機能のキーワード: crystallization chaperon, peptide-protein complex, ca2+ binding, peptide binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 127375.09

構造登録者

Ecsedi, P.,Gogl, G.,Nyitray, L. (登録日: 2019-10-15, 公開日: 2020-05-27, 最終更新日: 2024-01-31)

主引用文献

Ecsedi, P.,Gogl, G.,Hof, H.,Kiss, B.,Harmat, V.,Nyitray, L.
Structure Determination of the Transactivation Domain of p53 in Complex with S100A4 Using Annexin A2 as a Crystallization Chaperone.
Structure, 28:943-953.e4, 2020

PubMed Abstract: To fully understand the environmental factors that influence crystallization is an enormous task, therefore crystallographers are still forced to work "blindly" trying as many crystallizing conditions and mutations to improve crystal packing as possible. Numerous times these random attempts simply fail even when using state-of-the-art techniques. As an alternative, crystallization chaperones, having good crystal-forming properties, can be invoked. Today, the almost exclusively used such protein is the maltose-binding protein (MBP) and crystallographers need other widely applicable options. Here, we introduce annexin A2 (ANXA2), which has just as good, if not better, crystal-forming ability than the wild-type MBP. Using ANXA2 as heterologous fusion partner, we were able to solve the atomic resolution structure of a challenging crystallization target, the transactivation domain (TAD) of p53 in complex with the metastasis-associated protein S100A4. p53 TAD forms an asymmetric fuzzy complex with the symmetric S1004 and could interfere with its function.

PubMed: 32442400
DOI: 10.1016/j.str.2020.05.001

実験手法

X-RAY DIFFRACTION (3.1 Å)