Research output: Contribution to journal › Article
| Original language | English |
|---|---|
| Number of pages | 16 |
| Pages | 504-519 |
| Journal | Journal of Molecular Biology |
| Journal publication date | 20-Feb-2009 |
| Journal number | 2 |
| Volume | 386 |
| DOIs | |
| State | Published |
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.