6K7E

Crystal structure of MBPapo-Tim21 fusion protein with a 17-residue helical linker

6K7E の概要

• エントリーDOI: 10.2210/pdb6k7e/pdb
• 分子名称: Maltose/maltodextrin-binding periplasmic protein,Mitochondrial import inner membrane translocase subunit TIM21 (2 entities in total)
• 機能のキーワード: mbp, tim21, fusion protein, helical linker, translocase, sugar binding protein
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56719.40

構造登録者

Bala, S.,Shimada, A.,Kohda, D. (登録日: 2019-06-07, 公開日: 2019-09-18, 最終更新日: 2023-11-22)

主引用文献

Bala, S.,Shinya, S.,Srivastava, A.,Ishikawa, M.,Shimada, A.,Kobayashi, N.,Kojima, C.,Tama, F.,Miyashita, O.,Kohda, D.
Crystal contact-free conformation of an intrinsically flexible loop in protein crystal: Tim21 as the case study.
Biochim Biophys Acta Gen Subj, 1864:129418-129418, 2020

PubMed Abstract: In protein crystals, flexible loops are frequently deformed by crystal contacts, whereas in solution, the large motions result in the poor convergence of such flexible loops in NMR structure determinations. We need an experimental technique to characterize the structural and dynamic properties of intrinsically flexible loops of protein molecules.

PubMed: 31449839
DOI: 10.1016/j.bbagen.2019.129418

実験手法

X-RAY DIFFRACTION (1.534 Å)