Article
A remote prolyl isomerization controls domain assembly via a hydrogen bonding network.
Proceedings of the National Academy of Sciences of the United States of America - 28 Jul 2009
Weininger Ulrich, Jakob Roman P, Eckert Barbara, Schweimer Kristian, Schmid Franz X, Balbach Jochen
Abstract excerpt
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...
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