Structural highlights
Publication Abstract from PubMed
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.
Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site.,Pang A, Warren MJ, Pickersgill RW Acta Crystallogr D Biol Crystallogr. 2011 Feb;67(Pt 2):91-6. Epub 2011 Jan, 8. PMID:21245529[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pang A, Warren MJ, Pickersgill RW. Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site. Acta Crystallogr D Biol Crystallogr. 2011 Feb;67(Pt 2):91-6. Epub 2011 Jan, 8. PMID:21245529 doi:10.1107/S0907444910050201
