Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails.
The dra gene cluster of uropathogenic strains of Escherichia coli produces proteins involved in bacterial attachment to and invasion of the eukaryotic host tissues. The crystal structure of a construct of E. coli DraD possessing an additional C-terminal extension of 13 amino acids, including a His6 tag, has been solved at a resolution of 1.05 angstroms. The protein forms symmetric dimers through the exchange of the C-terminal beta-strands, which participate in the immunoglobulin-like beta-sandwich fold of each subunit. This structure confirms that DraD is able to act as an acceptor in the donor-strand complementation mechanism of fiber formation but, in contrast to DraE adhesin, its native sequence does not have a donor strand; therefore, DraD can only be located at the tip of the fiber.
Jedrzejczak
Robert
R
Synchrotron Radiation Research Section, MCL, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA.
Dauter
Zbigniew
Z
Dauter
Mirosława
M
Piatek
Rafał
R
Zalewska
Beata
B
Mróz
Marta
M
Bury
Katarzyna
K
Nowicki
Bogdan
B
Kur
Józef
J
D018830:Adhesins, Escherichia coli / Q000737:chemistry*; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000737:chemistry* / Q000472:pathogenicity; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D005816:Genetic Complementation Test; D006639:Histidine / Q000737:chemistry; D007136:Immunoglobulins / Q000737:chemistry; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D011487:Protein Conformation
D018830:Adhesins, Escherichia coli; D029968:Escherichia coli Proteins; C471213:His-His-His-His-His-His; D007136:Immunoglobulins; D009842:Oligopeptides; D006639:Histidine