1rxl
|
Solution structure of the engineered protein Afae-dsc
OverviewOverview
Pathogenic bacteria possess adhesion protein complexes that play essential, roles in targeting host cells and in propagating infection. Although each, family of adhesion proteins is generally associated with a specific human, disease, the Dr family from Escherichia coli is a notable exception, as, its members are associated with both diarrheal and urinary tract, infections. These proteins are reported to form both fimbrial and, afimbrial structures at the bacterial cell surface and target a common, host cell receptor, the decay-accelerating factor (DAF or CD55). Using the, newly solved three-dimensional structure of AfaE, we have constructed a, robust atomic resolution model that reveals the structural basis for, assembly by donor strand complementation and for the architecture of, capped surface fibers.
About this StructureAbout this Structure
1RXL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
An atomic resolution model for assembly, architecture, and function of the Dr adhesins., Anderson KL, Billington J, Pettigrew D, Cota E, Simpson P, Roversi P, Chen HA, Urvil P, du Merle L, Barlow PN, Medof ME, Smith RA, Nowicki B, Le Bouguenec C, Lea SM, Matthews S, Mol Cell. 2004 Aug 27;15(4):647-57. PMID:15327779
Page seeded by OCA on Wed Nov 21 01:56:08 2007
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Escherichia coli
- Single protein
- Anderson, K.L.
- Barlow, P.N.
- Billington, J.
- Bouguenec, C.Le.
- Chen, H.A.
- Cota, E
- Lea, S.M.
- Matthews, S.
- Medof, M.E.
- Merle, L.du.
- Nowicki, B.
- Pettigrew, D.
- Roversi, P.
- Simpson, P.
- Smith, R.A.
- Urvil, P.
- Afae
- Afimbrial sheath
- Daec
- Daf
- Donor strand complemented
- Ig-like domain
- Nmr
- Upec