6V3Z

Structure of Salmonella enteritidis Sen1395

Summary for 6V3Z

• Entry DOI: 10.2210/pdb6v3z/pdb
• Descriptor: Sen1395 (2 entities in total)
• Functional Keywords: muramidase lysozyme-like peptidoglycan-binding, protein transport
• Biological source: Salmonella enteritidis
• Total number of polymer chains: 2
• Total formula weight: 44914.78

Authors

Galan, J.E.,Lara-Tejero, M. (deposition date: 2019-11-27, release date: 2020-01-29, Last modification date: 2024-04-03)

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

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: 31958059
DOI: 10.7554/eLife.53473

Experimental method

X-RAY DIFFRACTION (1.9 Å)