2AXW

Structure of DraD invasin from uropathogenic Escherichia coli

2AXW の概要

• エントリーDOI: 10.2210/pdb2axw/pdb
• 分子名称: DraD invasin, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: homodimer, beta-sandwich, immunoglobulin-like fold, swapped c-terminal strands, cell invasion
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29554.13

構造登録者

Jedrzejczak, R.,Dauter, Z.,Dauter, M.,Piatek, R.,Zalewska, B.,Mroz, M.,Bury, K.,Nowicki, B.,Kur, J. (登録日: 2005-09-06, 公開日: 2005-11-01, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.05 Å)