Difference between revisions of "Part:BBa K3128031"
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OmpX consists of an eight-stranded antiparallel all-next-neighbor beta barrel. The structure shows two girdles of aromatic amino acid residues and a ribbon of nonpolar residues that attach to the membrane interior. The core of the barrel consists of an extended hydrogen-bonding network of highly conserved residues. OmpX thus resembles an inverse micelle. (1) | OmpX consists of an eight-stranded antiparallel all-next-neighbor beta barrel. The structure shows two girdles of aromatic amino acid residues and a ribbon of nonpolar residues that attach to the membrane interior. The core of the barrel consists of an extended hydrogen-bonding network of highly conserved residues. OmpX thus resembles an inverse micelle. (1) | ||
| − | [[ | + | [[File:OmpX protein structure.jpeg|200px|thumb|left|Figure 1]] |
==References== | ==References== | ||
Revision as of 11:58, 23 September 2019
Outer Membrane Protein X (OmpX) WT gene
The integral outer membrane protein X (OmpX) from Escherichia coli belongs to a family of highly conserved bacterial proteins. Its role is to promote bacterial adhesion and entry into mammalian cells. These proteins have a role in the resistance against attack by the human complement system.(1)
Structure
OmpX consists of an eight-stranded antiparallel all-next-neighbor beta barrel. The structure shows two girdles of aromatic amino acid residues and a ribbon of nonpolar residues that attach to the membrane interior. The core of the barrel consists of an extended hydrogen-bonding network of highly conserved residues. OmpX thus resembles an inverse micelle. (1)
References
(1) Vogt, J., Schulz G. The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. 1999
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]