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.
Original language | English |
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Pages (from-to) | 504-519 |
Number of pages | 16 |
Journal | Journal of Molecular Biology |
Volume | 386 |
Issue number | 2 |
DOIs | |
Publication status | Published - 20 Feb 2009 |
Keywords
- SufI
- FtsP
- Tat
- cupredoxin
- X-ray crystallography
- GREEN FLUORESCENT PROTEIN
- PENICILLIN-BINDING PROTEIN-3
- TWIN-ARGININE TRANSLOCASE
- SIGNAL PEPTIDE
- 3 DIMENSIONS
- PATHWAY
- EXPORT
- CUEO
- INVOLVEMENT
- TRANSPORT