2AXW

Structure of DraD invasin from uropathogenic Escherichia coli

Summary for 2AXW

• Entry DOI: 10.2210/pdb2axw/pdb
• Descriptor: DraD invasin, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: homodimer, beta-sandwich, immunoglobulin-like fold, swapped c-terminal strands, cell invasion
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 29554.13

Authors

Jedrzejczak, R.,Dauter, Z.,Dauter, M.,Piatek, R.,Zalewska, B.,Mroz, M.,Bury, K.,Nowicki, B.,Kur, J. (deposition date: 2005-09-06, release date: 2005-11-01, Last modification date: 2024-11-20)

Primary citation

Jedrzejczak, R.,Dauter, Z.,Dauter, M.,Piatek, R.,Zalewska, B.,Mroz, M.,Bury, K.,Nowicki, B.,Kur, J.
Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails.
Acta Crystallogr.,Sect.D, 62:157-164, 2006

PubMed Abstract: 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.

PubMed: 16421447
DOI: 10.1107/S0907444905036747

Experimental method

X-RAY DIFFRACTION (1.05 Å)