4RHR

Crystal structure of PltB

Summary for 4RHR

• Entry DOI: 10.2210/pdb4rhr/pdb
• Related: 4k6l
• Descriptor: Putative pertussis-like toxin subunit, ACETATE ION (3 entities in total)
• Functional Keywords: sugar binding motif, sugar binding, sugar, sugar binding protein
• Biological source: Salmonella enterica subsp. enterica serovar Typhi
• Total number of polymer chains: 5
• Total formula weight: 68407.15

Authors

Gao, X.,Wang, J.,Galan, J. (deposition date: 2014-10-02, release date: 2014-10-29, Last modification date: 2014-12-17)

Primary citation

Deng, L.,Song, J.,Gao, X.,Wang, J.,Yu, H.,Chen, X.,Varki, N.,Naito-Matsui, Y.,Galan, J.E.,Varki, A.
Host adaptation of a bacterial toxin from the human pathogen salmonella typhi.
Cell(Cambridge,Mass.), 159:1290-1299, 2014

PubMed Abstract: Salmonella Typhi is an exclusive human pathogen that causes typhoid fever. Typhoid toxin is a S. Typhi virulence factor that can reproduce most of the typhoid fever symptoms in experimental animals. Toxicity depends on toxin binding to terminally sialylated glycans on surface glycoproteins. Human glycans are unusual because of the lack of CMAH, which in other mammals converts N-acetylneuraminic acid (Neu5Ac) to N-glycolylneuraminic acid (Neu5Gc). Here, we report that typhoid toxin binds to and is toxic toward cells expressing glycans terminated in Neu5Ac (expressed by humans) over glycans terminated in Neu5Gc (expressed by other mammals). Mice constitutively expressing CMAH thus displaying Neu5Gc in all tissues are resistant to typhoid toxin. The atomic structure of typhoid toxin bound to Neu5Ac reveals the structural bases for its binding specificity. These findings provide insight into the molecular bases for Salmonella Typhi's host specificity and may help the development of therapies for typhoid fever.

PubMed: 25480294
DOI: 10.1016/j.cell.2014.10.057

Experimental method

X-RAY DIFFRACTION (2.079 Å)