Ontology highlight
ABSTRACT:
SUBMITTER: Alcorlo M
PROVIDER: S-EPMC6895207 | biostudies-literature | 2019 Dec
REPOSITORIES: biostudies-literature
Alcorlo Martín M Dik David A DA De Benedetti Stefania S Mahasenan Kiran V KV Lee Mijoon M Domínguez-Gil Teresa T Hesek Dusan D Lastochkin Elena E López Daniel D Boggess Bill B Mobashery Shahriar S Hermoso Juan A JA
Nature communications 20191205 1
SPOR domains are widely present in bacterial proteins that recognize cell-wall peptidoglycan strands stripped of the peptide stems. This type of peptidoglycan is enriched in the septal ring as a product of catalysis by cell-wall amidases that participate in the separation of daughter cells during cell division. Here, we document binding of synthetic denuded glycan ligands to the SPOR domain of the lytic transglycosylase RlpA from Pseudomonas aeruginosa (SPOR-RlpA) by mass spectrometry and struct ...[more]