6B8C

Crystal structure of NlpC/p60 domain of peptidoglycan hydrolase SagA

Summary for 6B8C

• Entry DOI: 10.2210/pdb6b8c/pdb
• Descriptor: NLP/P60 (2 entities in total)
• Functional Keywords: peptidoglycan endopeptidase, hydrolase
• Biological source: Enterococcus faecium (Streptococcus faecium)
• Total number of polymer chains: 1
• Total formula weight: 15715.21

Authors

Kim, B.,Oren, D.A.,Hang, H.C. (deposition date: 2017-10-06, release date: 2019-01-16, Last modification date: 2023-10-04)

Primary citation

Kim, B.,Wang, Y.C.,Hespen, C.W.,Espinosa, J.,Salje, J.,Rangan, K.J.,Oren, D.A.,Kang, J.Y.,Pedicord, V.A.,Hang, H.C.
Enterococcus faeciumsecreted antigen A generates muropeptides to enhance host immunity and limit bacterial pathogenesis.
Elife, 8:-, 2019

PubMed Abstract: We discovered that (), a ubiquitous commensal bacterium, and its secreted peptidoglycan hydrolase (SagA) were sufficient to enhance intestinal barrier function and pathogen tolerance, but the precise biochemical mechanism was unknown. Here we show has unique peptidoglycan composition and remodeling activity through SagA, which generates smaller muropeptides that more effectively activates nucleotide-binding oligomerization domain-containing protein 2 (NOD2) in mammalian cells. Our structural and biochemical studies show that SagA is a NlpC/p60-endopeptidase that preferentially hydrolyzes crosslinked Lys-type peptidoglycan fragments. SagA secretion and NlpC/p60-endopeptidase activity was required for enhancing probiotic bacteria activity against pathogenesis . Our results demonstrate that the peptidoglycan composition and hydrolase activity of specific microbiota species can activate host immune pathways and enhance tolerance to pathogens.

PubMed: 30969170
DOI: 10.7554/eLife.45343

Experimental method

X-RAY DIFFRACTION (2.403 Å)