at Google ScholarTitle data
Weininger, Ulrich ; Jakob, Roman P. ; Eckert, Barbara ; Schweimer, Kristian ; Schmid, Franz X. ; Balbach, Jochen:
A remote prolyl isomerization controls domain assembly via a hydrogen bonding network.
In: Proceedings of the National Academy of Sciences of the United States of America.
Vol. 106
(2009)
Issue 30
.
- 12335 -12340.
ISSN 1091-6490
DOI: https://doi.org/10.1073/pnas.0902102106
Abstract in another language
Prolyl cis/trans isomerizations determine the rates of protein folding reactions and can serve as molecular switches and timers. In the gene-3-protein of filamentous phage, Pro-213 trans → cis isomerization in a hinge region controls the assembly of the 2 domains N1 and N2 and, in reverse, the activation of the phage for infection. We elucidated the structural and energetic basis of this proline-limited domain assembly at the level of individual residues by real-time 2D NMR. A local cluster of inter-domain hydrogen bonds, remote from Pro-213, is stabilized up to 3,000-fold by trans → cis isomerization. This network of hydrogen bonds mediates domain assembly and is connected with Pro-213 by rigid backbone segments. Thus, proline cis/trans switching is propagated in a specific and directional fashion to change the protein structure and stability at a distant position.