2K39

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

Summary for 2K39

• Entry DOI: 10.2210/pdb2k39/pdb
• Descriptor: Ubiquitin (1 entity in total)
• Functional Keywords: ubiquitin, rdc, residual dipolar coupling, cytoplasm, nucleus, ubl conjugation, signaling protein
• Biological source: Xenopus laevis (African clawed frog)
• Total number of polymer chains: 1
• Total formula weight: 8576.83

Authors

Lange, O.F.,Lakomek, N.A.,Fares, C.,Schroder, G.,Walter, K.,Becker, S.,Meiler, J.,Grubmuller, H.,Griesinger, C.,de Groot, B.L. (deposition date: 2008-04-25, release date: 2008-06-24, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR