Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site

Pang, Allan, Warren, Martin J. ORCID: https://orcid.org/0000-0002-6028-6456 and Pickersgill, Richard W. (2011) Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site. Acta Crystallographica Section D: Biological Crystallography, 67 (2). pp. 91-96. ISSN 0907-4449

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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.

Item Type:	Article
Uncontrolled Keywords:	4fe-4s cluster-binding site,citrobacter freundii,pdut,propanediol metabolism,structural biology ,/dk/atira/pure/subjectarea/asjc/1300/1315
Faculty \ School:	Faculty of Science
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	20 Sep 2022 15:30
Last Modified:	25 Oct 2022 00:14
URI:	https://ueaeprints.uea.ac.uk/id/eprint/88514
DOI:	10.1107/S0907444910050201

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