Ontology highlight
ABSTRACT:
SUBMITTER: Heß N
PROVIDER: S-EPMC5727136 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Heß Nathalie N Waldow Franziska F Kohler Thomas P TP Rohde Manfred M Kreikemeyer Bernd B Gómez-Mejia Alejandro A Hain Torsten T Schwudke Dominik D Vollmer Waldemar W Hammerschmidt Sven S Gisch Nicolas N
Nature communications 20171212 1
Teichoic acid (TA), a crucial cell wall constituent of the pathobiont Streptococcus pneumoniae, is bound to peptidoglycan (wall teichoic acid, WTA) or to membrane glycolipids (lipoteichoic acid, LTA). Both TA polymers share a common precursor synthesis pathway, but differ in the final transfer of the TA chain to either peptidoglycan or a glycolipid. Here, we show that LTA exhibits a different linkage conformation compared to WTA, and identify TacL (previously known as RafX) as a putative lipotei ...[more]