In Mycobacterium tuberculosis, the activity of a protein lysine acetyltransferase (PAT) is allosterically regulated by cAMP binding to a domain fused to the catalytic domain. Now the crystal structures of the autoinhibited and cAMP-activated PAT, along with biochemical analysis, reveal how allosteric regulation between independent protein domains can evolve.
- Ho Jun Lee
- P Therese Lang
- Tom Alber
