Long range dynamic effects of point-mutations trap a response regulator in an active conformation.
When a point-mutation in a protein elicits a functional change, it is most common to assign this change to local structural perturbations. Here we show that point-mutations, distant from an essential highly dynamic kinase recognition loop in the response regulator Spo0F, lock this loop in an active conformation. This 'conformational trapping' results in functionally hyperactive Spo0F. Consequently, point-mutations are seen to affect functionally critical motions both close to and far from the mutational site.
Bobay
Benjamin G
BG
Department of Molecular and Structural Biochemistry, North Carolina State University, NC 27695, USA.
Thompson
Richele J
RJ
Hoch
James A
JA
Cavanagh
John
J
D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D017354:Point Mutation; D025341:Principal Component Analysis; D011487:Protein Conformation; D015290:Second Messenger Systems / Q000235:genetics; D015398:Signal Transduction / Q000235:genetics; D013816:Thermodynamics
D001426:Bacterial Proteins; D050505:Mutant Proteins; C080951:Spo0F protein, Bacillus subtilis