RRC ID 4952
Author Arnold T, Zeth K, Linke D.
Title Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain.
Journal J Biol Chem
Abstract Colicins are plasmid-encoded toxic proteins produced by Escherichia coli strains to kill other E. coli strains that lack the corresponding immunity protein. Colicins intrude into the host cell by exploiting existing transport, diffusion, or efflux systems. We have traced the way colicin S4 takes to execute its function and show that it interacts specifically with OmpW, OmpF, and the Tol system before it inserts its pore-forming domain into the cytoplasmic membrane. The common structural architecture of colicins comprises a translocation, a receptor-binding, and an activity domain. We have solved the crystal structure of colicin S4 to a resolution of 2.5 A, which shows a remarkably compact domain arrangement of four independent domains, including a unique domain duplication of the receptor-binding domain. Finally, we have determined the residues responsible for binding to the receptor OmpW by mutating exposed charged residues in one or both receptor-binding domains.
Volume 284(10)
Pages 6403-13
Published 2009-3-6
DOI 10.1074/jbc.M808504200
PII S0021-9258(20)32668-5
PMID 19056731
PMC PMC2649078
MeSH Bacterial Outer Membrane Proteins / chemistry Bacterial Outer Membrane Proteins / genetics Bacterial Outer Membrane Proteins / metabolism Colicins / chemistry* Colicins / genetics Colicins / metabolism Crystallography, X-Ray Escherichia coli / chemistry* Escherichia coli / genetics Escherichia coli / metabolism Escherichia coli Proteins / chemistry Escherichia coli Proteins / genetics Escherichia coli Proteins / metabolism Porins / chemistry Porins / genetics Porins / metabolism Protein Structure, Tertiary / physiology Protein Transport Structure-Activity Relationship
IF 4.238
Times Cited 31
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Prokaryotes E. coli ME9062(BW25113)