PMID:10545325
| Citation |
Vogt, J and Schulz, GE (1999) The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. Structure 7:1301-9 |
|---|---|
| Abstract |
The integral outer membrane protein X (OmpX) from Escherichia coli belongs to a family of highly conserved bacterial proteins that promote bacterial adhesion to and entry into mammalian cells. Moreover, these proteins have a role in the resistance against attack by the human complement system. Here we present the first crystal structure of a member of this family. |
| Links | |
| Keywords |
Amino Acid Sequence; Animals; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Crystallography, X-Ray; Electrochemistry; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli/pathogenicity; Escherichia coli Proteins; Humans; Hydrolases; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Conformation; Sequence Homology, Amino Acid; Virulence |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.