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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
Journal number2
Volume386
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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