The Escherichia coli Cell Division Protein and Model Tat Substrate Sufl (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like Structure

Michael Tarry, S. J. Ryan Arends, Pietro Roversi, Evan Piette, Frank Sargent, Ben C. Berks, David S. Weiss, Susan M. Lea

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    Abstract

    The Escherichia coli protein SufI (FtsP) has recently been proposed to be a component of the cell division apparatus. The SufI protein is also in widespread experimental use as a model substrate in studies of the Tat (twin arginine translocation) protein transport system. We have used SufI-GFP (green fluorescent protein) fusions to show that SufI localizes to the septal ring in the dividing cell. We have also determined the structure of SufI by X-ray crystallography to a resolution of 1.9 angstrom. SufI is structurally related to the multicopper oxidase superfamily but lacks metal cofactors. The structure of SufI suggests it serves a scaffolding rather than an enzymatic role in the septal ring and reveals regions of the protein likely to be involved in the protein-protein interactions required to assemble SufI at the septal ring. (C) 2009 Elsevier Ltd. All rights reserved.

    Original languageEnglish
    Pages (from-to)504-519
    Number of pages16
    JournalJournal of Molecular Biology
    Volume386
    Issue number2
    DOIs
    Publication statusPublished - 20 Feb 2009

    Keywords

    • SufI
    • FtsP
    • Tat
    • cupredoxin
    • X-ray crystallography
    • GREEN FLUORESCENT PROTEIN
    • PENICILLIN-BINDING PROTEIN-3
    • TWIN-ARGININE TRANSLOCASE
    • SIGNAL PEPTIDE
    • 3 DIMENSIONS
    • PATHWAY
    • EXPORT
    • CUEO
    • INVOLVEMENT
    • TRANSPORT

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