Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein.

ABSTRACT: Recently, progress has been made toward understanding the functional diversity of bacterial microcompartment (MCP) systems, which serve as protein-based metabolic organelles in diverse microbes. New types of MCPs have been identified, including the glycyl-radical propanediol (Grp) MCP. Within these elaborate protein complexes, BMC-domain shell proteins [bacterial microcompartment (in reference to the shell protein domain)] assemble to form a polyhedral barrier that encapsulates the enzymatic contents of the MCP. Interestingly, the Grp MCP contains a number of shell proteins with unusual sequence features. GrpU is one such shell protein whose amino acid sequence is particularly divergent from other members of the BMC-domain superfamily of proteins that effectively defines all MCPs. Expressi

SUBMITTER: Thompson MC 

PROVIDER: S-EPMC4175982 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature