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

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

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Authors

  • 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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Original languageEnglish
Pages504-519
Number of pages16
JournalJournal of Molecular Biology
Journal publication date20 Feb 2009
Volume386
Issue2
DOIs
StatePublished

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.

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