6V40
Structure of Salmonella Typhi TtsA
Summary for 6V40
| Entry DOI | 10.2210/pdb6v40/pdb |
| Descriptor | PG_binding_3 domain-containing protein, 2,6-DIAMINOPIMELIC ACID, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
| Functional Keywords | muramidase lysozyme-like peptidoglycan-binding, protein transport |
| Biological source | Salmonella typhi |
| Total number of polymer chains | 4 |
| Total formula weight | 90327.76 |
| Authors | Galan, J.E.,Lara-Tejero, M. (deposition date: 2019-11-27, release date: 2020-01-29, Last modification date: 2023-11-15) |
| Primary citation | Geiger, T.,Lara-Tejero, M.,Xiong, Y.,Galan, J.E. Mechanisms of substrate recognition by a typhoid toxin secretion-associated muramidase. Elife, 9:-, 2020 Cited by PubMed Abstract: Typhoid toxin is a virulence factor for the bacterial pathogen Typhi, which causes typhoid fever in humans. After its synthesis by intracellular bacteria, typhoid toxin is secreted into the lumen of the -containing vacuole by a secretion mechanism strictly dependent on TtsA, a specific muramidase that facilitates toxin transport through the peptidoglycan layer. Here we show that substrate recognition by TtsA depends on a discrete domain within its carboxy terminus, which targets the enzyme to the bacterial poles to recognize YcbB-edited peptidoglycan. Comparison of the atomic structures of TtsA bound to its substrate and that of a close homolog with different specificity identified specific determinants involved in substrate recognition. Combined with structure-guided mutagenesis and in vitro and in vivo crosslinking experiments, this study provides an unprecedented view of the mechanisms by which a muramidase recognizes its peptidoglycan substrate to facilitate protein secretion. PubMed: 31958059DOI: 10.7554/eLife.53473 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.104 Å) |
Structure validation
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