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6lnw
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of accessory secretory protein 1,2 and 3 in Streptococcus pneumoniae== | |
| + | <StructureSection load='6lnw' size='340' side='right'caption='[[6lnw]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6lnw]] is a 3 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LNW FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6lnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lnw OCA], [http://pdbe.org/6lnw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lnw RCSB], [http://www.ebi.ac.uk/pdbsum/6lnw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lnw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6lnw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Feng, Z]] | ||
[[Category: Guo, C]] | [[Category: Guo, C]] | ||
[[Category: Zuo, G]] | [[Category: Zuo, G]] | ||
| - | [[Category: | + | [[Category: Complex]] |
| + | [[Category: Transport protein]] | ||
Revision as of 09:15, 26 February 2020
Crystal structure of accessory secretory protein 1,2 and 3 in Streptococcus pneumoniae
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