A molecular Swiss army knife: OmpA structure, function and expression.
The OmpA outer membrane protein of Escherichia coli and other enterobacteria is a multifaceted protein. This protein is expressed to very high levels and ompA is tightly regulated at the posttranscriptional level. It can function as an adhesin and invasin, participate in biofilm formation, act as both an immune target and evasin, and serves as a receptor for several bacteriophages. Many of these properties are due to four short protein loops that emanate from the protein to the outside of the cell. Herein it is described how the structure of this protein relates to its many functions.
Smith
Stephen G J
SG
Department of Clinical Microbiology, Trinity College Dublin, St James's Hospital, Dublin, Ireland. sgsmith@tcd.ie
Mahon
Vivienne
V
Lambert
Matthew A
MA
Fagan
Robert P
RP
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology / Q000502:physiology*; D004926:Escherichia coli / Q000737:chemistry* / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology / Q000502:physiology*; D015964:Gene Expression Regulation, Bacterial; D008958:Models, Molecular; D008969:Molecular Sequence Data
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C078167:OMPA outer membrane proteins