3PAC

Crystal structure of PduT a trimeric bacterial microcompartment protein with 4Fe-4S cluster binding site

Summary for 3PAC

• Entry DOI: 10.2210/pdb3pac/pdb
• Descriptor: Shell protein (2 entities in total)
• Functional Keywords: bmc domain, shell protein, electron transport
• Biological source: Citrobacter freundii
• Total number of polymer chains: 1
• Total formula weight: 21226.57

Authors

Pang, A.H.,Warren, M.J.,Pickersgill, R.W. (deposition date: 2010-10-19, release date: 2010-12-01, Last modification date: 2024-03-20)

Primary citation

Pang, A.,Warren, M.J.,Pickersgill, R.W.
Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site
Acta Crystallogr.,Sect.D, 67:91-96, 2011

PubMed Abstract: 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.

PubMed: 21245529
DOI: 10.1107/S0907444910050201

Experimental method

X-RAY DIFFRACTION (1.86 Å)