Chapter title |
High-Pressure NMR Spectroscopy Reveals Functional Sub-states of Ubiquitin and Ubiquitin-Like Proteins
|
---|---|
Chapter number | 10 |
Book title |
High Pressure Bioscience
|
Published in |
Sub cellular biochemistry, January 2015
|
DOI | 10.1007/978-94-017-9918-8_10 |
Pubmed ID | |
Book ISBNs |
978-9-40-179917-1, 978-9-40-179918-8
|
Authors |
Ryo Kitahara, Kitahara, Ryo |
Abstract |
High-pressure nuclear magnetic resonance (NMR) spectroscopy has revealed that ubiquitin has at least two high-energy states - an alternatively folded state N2 and a locally disordered state I - between the basic folded state N1 and totally unfolded U state. The high-energy states are conserved among ubiquitin-like post-translational modifiers, ubiquitin, NEDD8, and SUMO-2, showing the E1-E2-E3 cascade reaction. It is quite intriguing that structurally similar high-energy states are evolutionally conserved in the ubiquitin-like modifiers, and the thermodynamic stabilities vary among the proteins. To investigate atomic details of the high-energy states, a Q41N mutant of ubiquitin was created as a structural model of N2, which is 71 % populated even at atmospheric pressure. The convergent structure of the "pure" N2 state was obtained by nuclear Overhauser effect (NOE)-based structural analysis of the Q41N mutant at 2.5 kbar, where the N2 state is 97 % populated. The N2 state of ubiquitin is closely similar to the conformation of the protein bound to the ubiquitin-activating enzyme E1. The recognition of E1 by ubiquitin is best explained by conformational selection rather than by induced-fit motion. |
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