Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 105, Issue 31, Pages 10709-10714Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0709610105
Keywords
allostery; LOV domain; protein design; trp repressor; alpha helix
Categories
Funding
- NIGMS NIH HHS [R01 GM055694, R01 GM055694-12, R01 GM055694-11, R01 GM055694-13, R01 GM055694-10] Funding Source: Medline
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An understanding of how allostery, the conformational coupling of distant functional sites, arises in highly evolvable systems is of considerable interest in areas ranging from cell biology to protein design and signaling networks. We reasoned that the rigidity and defined geometry of an alpha-helical domain linker would make it effective as a conduit for allosteric signals. To test this idea, we rationally designed 12 fusions between the naturally photoactive LOV2 domain from Avena sativa phototropin 1 and the Escherichia coli trp repressor. When illuminated, one of the fusions selectively binds operator DNA and protects it from nuclease digestion. The ready success of our rational design strategy suggests that the helical allosteric lever arm is a general scheme for coupling the function of two proteins.
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