3H6J

Crystal structure of a putative neuraminidase from Pseudomonas aeruginosa

3H6J の概要

• エントリーDOI: 10.2210/pdb3h6j/pdb
• 関連するPDBエントリー: 3H71 3H72 3H73
• 分子名称: Neuraminidase (2 entities in total)
• 機能のキーワード: six-bladed beta-propeller, cell wall, glycosidase, hydrolase, peptidoglycan-anchor, secreted
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47157.98

構造登録者

Hsiao, Y.-S.,Tong, L. (登録日: 2009-04-23, 公開日: 2009-05-12, 最終更新日: 2024-02-21)

主引用文献

Hsiao, Y.-S.,Parker, D.,Ratner, A.J.,Prince, A.,Tong, L.
Crystal structures of respiratory pathogen neuraminidases
Biochem.Biophys.Res.Commun., 380:467-471, 2009

PubMed Abstract: Currently there is pressing need to develop novel therapeutic agents for the treatment of infections by the human respiratory pathogens Pseudomonas aeruginosa and Streptococcus pneumoniae. The neuraminidases of these pathogens are important for host colonization in animal models of infection and are attractive targets for drug discovery. To aid in the development of inhibitors against these neuraminidases, we have determined the crystal structures of the P. aeruginosa enzyme NanPs and S. pneumoniae enzyme NanA at 1.6 and 1.7A resolution, respectively. In situ proteolysis with trypsin was essential for the crystallization of our recombinant NanA. The active site regions of the two enzymes are strikingly different. NanA contains a deep pocket that is similar to that in canonical neuraminidases, while the NanPs active site is much more open. The comparative studies suggest that NanPs may not be a classical neuraminidase, and may have distinct natural substrates and physiological functions. This work represents an important step in the development of drugs to prevent respiratory tract colonization by these two pathogens.

PubMed: 19284989
DOI: 10.1016/j.bbrc.2009.01.108

実験手法

X-RAY DIFFRACTION (1.6 Å)