Reaction Products and the X-ray Structure of AmpDh2, a Virulence Determinant of Pseudomonas aeruginosa

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• 作者：Siseth Mart铆nez-Caballero ; Mijoon Lee ; Cecilia Artola-Recolons ; C茅sar Carrasco-L贸pez ; Dusan Hesek ; Edward Spink ; Elena Lastochkin ; Weilie Zhang ; Lance M. Hellman ; Bill Boggess ; Shahriar Mobashery ; Juan A. Hermoso
• 刊名：The Journal of the American Chemical Society
• 出版年：2013
• 出版时间：July 17, 2013
• 年：2013
• 卷：135
• 期：28
• 页码：10318-10321
• 全文大小：365K
• 年卷期：v.135,no.28(July 17, 2013)
• ISSN：1520-5126

文摘

The zinc protease AmpDh2 is a virulence determinant of Pseudomonas aeruginosa, a problematic human pathogen. The mechanism of how the protease manifests virulence is not known, but it is known that it turns over the bacterial cell wall. The reaction of AmpDh2 with the cell wall was investigated, and nine distinct turnover products were characterized by LC/MS/MS. The enzyme turns over both the cross-linked and noncross-linked cell wall. Three high-resolution X-ray structures, the apo enzyme and two complexes with turnover products, were solved. The X-ray structures show how the dimeric protein interacts with the inner leaflet of the bacterial outer membrane and that the two monomers provide a more expansive surface for recognition of the cell wall. This binding surface can accommodate the 3D solution structure of the cross-linked cell wall.