2K39

Recognition dynamics up to microseconds revealed from RDC derived ubiquitin ensemble in solution

2K39 の概要

• エントリーDOI: 10.2210/pdb2k39/pdb
• 分子名称: Ubiquitin (1 entity in total)
• 機能のキーワード: ubiquitin, rdc, residual dipolar coupling, cytoplasm, nucleus, ubl conjugation, signaling protein
• 由来する生物種: Xenopus laevis (African clawed frog)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8576.83

構造登録者

Lange, O.F.,Lakomek, N.A.,Fares, C.,Schroder, G.,Walter, K.,Becker, S.,Meiler, J.,Grubmuller, H.,Griesinger, C.,de Groot, B.L. (登録日: 2008-04-25, 公開日: 2008-06-24, 最終更新日: 2024-05-01)

主引用文献

Lange, O.F.,Lakomek, N.A.,Fares, C.,Schroder, G.F.,Walter, K.F.,Becker, S.,Meiler, J.,Grubmuller, H.,Griesinger, C.,de Groot, B.L.
Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution.
Science, 320:1471-1475, 2008

PubMed Abstract: Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost.

PubMed: 18556554
DOI: 10.1126/science.1157092

実験手法

SOLUTION NMR