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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 A. 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.

Original publication

DOI

10.1016/j.jmb.2008.12.043

Type

Journal article

Journal

J Mol Biol

Publication Date

20/02/2009

Volume

386

Pages

504 - 519

Keywords

Artificial Gene Fusion, Cell Division, Crystallography, X-Ray, Escherichia coli, Escherichia coli Proteins, Genes, Reporter, Green Fluorescent Proteins, Models, Molecular, Protein Structure, Tertiary, Recombinant Fusion Proteins