6LNW

Crystal structure of accessory secretory protein 1,2 and 3 in Streptococcus pneumoniae

Summary for 6LNW

• Entry DOI: 10.2210/pdb6lnw/pdb
• Descriptor: Accessory secretory protein Asp1, Accessory secretory protein Asp2, Accessory secretory protein Asp3, ... (4 entities in total)
• Functional Keywords: complex, transport protein
• Biological source: Streptococcus pneumoniae TIGR4; More
• Total number of polymer chains: 3
• Total formula weight: 139253.50

Authors

Guo, C.,Feng, Z.,Zuo, G. (deposition date: 2020-01-02, release date: 2020-02-26, Last modification date: 2023-11-29)

Primary citation

Guo, C.,Feng, Z.,Zuo, G.,Jiang, Y.L.,Zhou, C.Z.,Chen, Y.,Hou, W.T.
Structural and functional insights into the Asp1/2/3 complex mediated secretion of pneumococcal serine-rich repeat protein PsrP.
Biochem.Biophys.Res.Commun., 524:784-790, 2020

PubMed Abstract: 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 Å. 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.

PubMed: 32037091
DOI: 10.1016/j.bbrc.2020.01.146

Experimental method

X-RAY DIFFRACTION (2.9 Å)