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

Allan Pang, Martin J. Warren, Richard W. Pickersgill

Research output: Contribution to journalArticlepeer-review

51 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)91-96
Number of pages6
JournalActa Crystallographica Section D: Biological Crystallography
Volume67
Issue number2
DOIs
Publication statusPublished - Feb 2011

Keywords

  • 4Fe-4S cluster-binding site
  • Citrobacter freundii
  • PduT
  • propanediol metabolism

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