The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (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

doi:10.1016/j.jmb.2008.12.043

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

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The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (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 and Susan M Lea

Journal of molecular biology, Vol.386(2), pp.504-519

02/20/2009

DOI: 10.1016/j.jmb.2008.12.043

PMCID: PMC2661564

PMID: 19135451

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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 Å. 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.

X-ray crystallography

GFP, green fluorescent protein

SufI

Tat, twin arginine translocation

LB0N, LB without 10g NaCl per liter

Tat

cupredoxin

T1, mononuclear type I

FtsP

NCS, non-crystallographic symmetry

Details

Title: Subtitle: The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like Structure
Creators: Michael Tarry - College of Life Sciences, University of Dundee, Scotland DD1 5EH
S.J. Ryan Arends - College of Life Sciences, University of Dundee, Scotland DD1 5EH
Pietro Roversi - College of Life Sciences, University of Dundee, Scotland DD1 5EH
Evan Piette - College of Life Sciences, University of Dundee, Scotland DD1 5EH
Frank Sargent - College of Life Sciences, University of Dundee, Scotland DD1 5EH
Ben C Berks - College of Life Sciences, University of Dundee, Scotland DD1 5EH
David S Weiss - College of Life Sciences, University of Dundee, Scotland DD1 5EH
Susan M Lea - College of Life Sciences, University of Dundee, Scotland DD1 5EH
Resource Type: Journal article
Publication Details: Journal of molecular biology, Vol.386(2), pp.504-519
DOI: 10.1016/j.jmb.2008.12.043
PMID: 19135451
PMCID: PMC2661564
NLM abbreviation: J Mol Biol
ISSN: 0022-2836
eISSN: 1089-8638
Publisher: Elsevier
Language: English
Date published: 02/20/2009
Academic Unit: Microbiology and Immunology
Record Identifier: 9984001204002771

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