Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site.
Propanediol metabolism in Citrobacter freundii occurs within a metabolosome, a subcellular proteinaceous bacterial microcompartment. The propanediol-utilization (Pdu) microcompartment shell is constructed from thousands of hexagonal-shaped protein complexes made from seven different types of protein subunit. Here, the structure of the bacterial microcompartment protein PduT, which has a tandem structural repeat within the subunit and forms trimers with pseudo-hexagonal symmetry, is reported. This trimeric assembly forms a flat approximately hexagonally shaped disc with a central pore that is suitable for a 4Fe-4S cluster. The essentially cubic shaped 4Fe-4S cluster conforms to the threefold symmetry of the trimer with one free iron, the role of which could be to supply electrons to an associated microcompartment enzyme, PduS.
School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London E1 4NS, England.
Allan
A
Pang
Martin J
MJ
Warren
Richard W
RW
Pickersgill
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D016971:Citrobacter freundii / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D007501:Iron / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D013455:Sulfur / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D013455:Sulfur; D007501:Iron