2axw
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(New page: 200px<br /><applet load="2axw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2axw, resolution 1.05Å" /> '''Structure of DraD in...)
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Revision as of 16:12, 29 January 2008
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Structure of DraD invasin from uropathogenic Escherichia coli
Overview
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.
About this Structure
2AXW is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
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
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