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Publication Abstract from PubMed

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.

Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails.,Jedrzejczak R, Dauter Z, Dauter M, Piatek R, Zalewska B, Mroz M, Bury K, Nowicki B, Kur J Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):157-64. Epub 2006, Jan 18. PMID:16421447^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.