3QRA

The crystal structure of Ail, the attachment invasion locus protein of Yersinia pestis

Summary for 3QRA

• Entry DOI: 10.2210/pdb3qra/pdb
• Related: 3QRC
• Descriptor: Attachment invasion locus protein, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (3 entities in total)
• Functional Keywords: beta-barrel protein, attachment and invasion virulence, laminin, heparin, cell invasion
• Biological source: Yersinia pestis
• Total number of polymer chains: 1
• Total formula weight: 19768.66

Authors

Yamashita, S.,Lukacik, P.,Noinaj, N.,Buchanan, S.K. (deposition date: 2011-02-17, release date: 2011-11-23, Last modification date: 2023-09-13)

Primary citation

Yamashita, S.,Lukacik, P.,Barnard, T.J.,Noinaj, N.,Felek, S.,Tsang, T.M.,Krukonis, E.S.,Hinnebusch, B.J.,Buchanan, S.K.
Structural Insights into Ail-Mediated Adhesion in Yersinia pestis.
Structure, 19:1672-1682, 2011

PubMed Abstract: Ail is an outer membrane protein from Yersinia pestis that is highly expressed in a rodent model of bubonic plague, making it a good candidate for vaccine development. Ail is important for attaching to host cells and evading host immune responses, facilitating rapid progression of a plague infection. Binding to host cells is important for injection of cytotoxic Yersinia outer proteins. To learn more about how Ail mediates adhesion, we solved two high-resolution crystal structures of Ail, with no ligand bound and in complex with a heparin analog called sucrose octasulfate. We identified multiple adhesion targets, including laminin and heparin, and showed that a 40 kDa domain of laminin called LG4-5 specifically binds to Ail. We also evaluated the contribution of laminin to delivery of Yops to HEp-2 cells. This work constitutes a structural description of how a bacterial outer membrane protein uses a multivalent approach to bind host cells.

PubMed: 22078566
DOI: 10.1016/j.str.2011.08.010

Experimental method

X-RAY DIFFRACTION (1.801 Å)