Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution.
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.
Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Oliver F
OF
Lange
Nils-Alexander
NA
Lakomek
Christophe
C
Farès
Gunnar F
GF
Schröder
Korvin F A
KF
Walter
Stefan
S
Becker
Jens
J
Meiler
Helmut
H
Grubmüller
Christian
C
Griesinger
Bert L
BL
de Groot
D020816:Amino Acid Motifs; D000818:Animals; D016880:Anisotropy; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D018360:Crystallography, X-Ray; D019277:Entropy; D007700:Kinetics; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012996:Solutions; D025801:Ubiquitin / Q000737:chemistry* / Q000378:metabolism*; D014982:Xenopus laevis
D012996:Solutions; D025801:Ubiquitin