Crystal structure of the MecA degradation tag.

ABSTRACT: MecA is an adaptor protein that regulates the assembly and activity of the ATP-dependent ClpCP protease in Bacillus subtilis. MecA contains two domains. Although the amino-terminal domain of MecA recruits substrate proteins such as ComK and ComS, the carboxyl-terminal domain (residues 121-218) has dual roles in the regulation and function of ClpCP protease. MecA-(121-218) facilitates the assembly of ClpCP oligomer, which is required for the protease activity of ClpCP. This domain was identified to be a non-recycling degradation tag that targets heterologous fusion proteins to the ClpCP protease for degradation. To elucidate the mechanism of MecA, we determined the crystal structure of MecA-(121-218) at 2.2 A resolution, which reveals a previously uncharacterized alpha/beta fold. Structure-

SUBMITTER: Wang F 

PROVIDER: S-EPMC2797205 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature