View source for 6lnw


==Crystal structure of accessory secretory protein 1,2 and 3 in Streptococcus pneumoniae==
<StructureSection load='6lnw' size='340' side='right'caption='[[6lnw]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lnw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LNW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6lnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lnw OCA], [https://pdbe.org/6lnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lnw RCSB], [https://www.ebi.ac.uk/pdbsum/6lnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lnw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2UR88_STRPN A0A0H2UR88_STRPN] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:32037091</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lnw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae TIGR4]]
[[Category: Feng Z]]
[[Category: Guo C]]
[[Category: Zuo G]]