Structural basis for type VI secreted peptidoglycan dl-endopeptidase function, specificity and neutralization in Serratia marcescens

Srikannathasan, V.; English, G.; Bui, N.K.; Trunk, K.; O'Rourke, P.E.F.; Rao, V.A.; Vollmer, W.; Coulthurst, S.J.; Hunter, W.N.

doi:10.1107/S0907444913022725

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 1
The specificity of Ssp1 and Ssp2. (a) Peptidoglycan from E. coli strain D456 was incubated with Ssp1, Ssp2 or no enzyme (control) followed by digestion with the muramidase Cellosyl and analysis of the resulting muropeptides by HPLC. Both Ssp1 and Ssp2 cleaved non-cross-linked (tri, tetra and penta) and cross-linked (tetratetra and tetrapenta) muropeptides between D-glutamate and meso-diaminopimelic acid (m-A₂pm), resulting in the disaccharide dipeptide (di) product. Ssp2 also produced a small amount of the disaccharide hexapeptide (hexa) product. (b) Proposed structures of the muropeptides separated in (a). The arrows indicate the cleavage sites of D-iGlu-m-A₂pm endopeptidases in peptidoglycan. GlcNAc, N-acetylglucosamine; MurNAc(r), N-acetylmuramitol; m-A₂pm, meso-diaminopimelic acid.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 69| Part 12| December 2013| Pages 2468-2482

https://doi.org/10.1107/S0907444913022725

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