Structural highlights
Function
A0A0K2E3A3_STRSU
Publication Abstract from PubMed
Synthesis of capsular polysaccharide (CPS), an important virulence factor of pathogenic bacteria, is modulated by the CpsBCD phosphoregulatory system in Streptococcus. Serine/threonine kinases (STKs, e.g. Stk1) can also regulate CPS synthesis, but the underlying mechanisms are unclear. Here, we identify a protein (CcpS) that is phosphorylated by Stk1 and modulates the activity of phosphatase CpsB in Streptococcus suis, thus linking Stk1 to CPS synthesis. The crystal structure of CcpS shows an intrinsically disordered region at its N-terminus, including two threonine residues that are phosphorylated by Stk1. The activity of phosphatase CpsB is inhibited when bound to non-phosphorylated CcpS. Thus, CcpS modulates the activity of phosphatase CpsB thereby altering CpsD phosphorylation, which in turn modulates the expression of the Wzx-Wzy pathway and thus CPS production.
A link between STK signalling and capsular polysaccharide synthesis in Streptococcus suis.,Tang J, Guo M, Chen M, Xu B, Ran T, Wang W, Ma Z, Lin H, Fan H Nat Commun. 2023 Apr 29;14(1):2480. doi: 10.1038/s41467-023-38210-4. PMID:37120581[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tang J, Guo M, Chen M, Xu B, Ran T, Wang W, Ma Z, Lin H, Fan H. A link between STK signalling and capsular polysaccharide synthesis in Streptococcus suis. Nat Commun. 2023 Apr 29;14(1):2480. PMID:37120581 doi:10.1038/s41467-023-38210-4
