Structural highlights
Publication Abstract from PubMed
The accessory sec system consisting of seven conserved components is commonly distributed among pathogenic Gram-positive bacteria for the secretion of serine-rich-repeat proteins (SRRPs). Asp1/2/3 protein complex in the system is responsible for both the O-acetylation of GlcNAc and delivering SRRPs to SecA2. However, the molecular mechanism of how Asp1/2/3 transport SRRPs remains unknown. Here, we report the complex structure of Asp1/2/3 from Streptococcus pneumoniae at 2.9 A. Further functional assays indicated that Asp1/2/3 can stimulate the ATPase activity of SecA2. In addition, the deletion of asp1/2/3 gene resulted in the accumulation of a secreted version of PsrP with an altered glycoform in protoplast fraction of the mutant cell, which suggested the modification/transport coupling of the substrate. Altogether, these findings not only provide structural basis for further investigations on the transport process of SRRPs, but also uncover the indispensable role of Asp1/2/3 in the accessory sec system.
Structural and functional insights into the Asp1/2/3 complex mediated secretion of pneumococcal serine-rich repeat protein PsrP.,Guo C, Feng Z, Zuo G, Jiang YL, Zhou CZ, Chen Y, Hou WT Biochem Biophys Res Commun. 2020 Feb 6. pii: S0006-291X(20)30229-1. doi:, 10.1016/j.bbrc.2020.01.146. PMID:32037091[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo C, Feng Z, Zuo G, Jiang YL, Zhou CZ, Chen Y, Hou WT. Structural and functional insights into the Asp1/2/3 complex mediated secretion of pneumococcal serine-rich repeat protein PsrP. Biochem Biophys Res Commun. 2020 Feb 6. pii: S0006-291X(20)30229-1. doi:, 10.1016/j.bbrc.2020.01.146. PMID:32037091 doi:http://dx.doi.org/10.1016/j.bbrc.2020.01.146
