2MUZ

ssNMR structure of a designed rocker protein

2MUZ の概要

• エントリーDOI: 10.2210/pdb2muz/pdb
• NMR情報: BMRB: 25236
• 分子名称: designed rocker protein (1 entity in total)
• 機能のキーワード: ssnmr, rocker protein, de novo desgin, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 11885.71

構造登録者

Wang, T.,Joh, N.,Wu, Y.,DeGrado, W.F.,Hong, M. (登録日: 2014-09-18, 公開日: 2014-12-24, 最終更新日: 2025-03-26)

主引用文献

Joh, N.H.,Wang, T.,Bhate, M.P.,Acharya, R.,Wu, Y.,Grabe, M.,Hong, M.,Grigoryan, G.,DeGrado, W.F.
De novo design of a transmembrane Zn2+-transporting four-helix bundle.
Science, 346:1520-1524, 2014

PubMed Abstract: The design of functional membrane proteins from first principles represents a grand challenge in chemistry and structural biology. Here, we report the design of a membrane-spanning, four-helical bundle that transports first-row transition metal ions Zn(2+) and Co(2+), but not Ca(2+), across membranes. The conduction path was designed to contain two di-metal binding sites that bind with negative cooperativity. X-ray crystallography and solid-state and solution nuclear magnetic resonance indicate that the overall helical bundle is formed from two tightly interacting pairs of helices, which form individual domains that interact weakly along a more dynamic interface. Vesicle flux experiments show that as Zn(2+) ions diffuse down their concentration gradients, protons are antiported. These experiments illustrate the feasibility of designing membrane proteins with predefined structural and dynamic properties.

PubMed: 25525248
DOI: 10.1126/science.1261172

実験手法

SOLUTION NMR