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| | <StructureSection load='6lnw' size='340' side='right'caption='[[6lnw]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='6lnw' size='340' side='right'caption='[[6lnw]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6lnw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpn Strpn]. 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> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SP_1762 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=170187 STRPN]), SP_1761 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=170187 STRPN]), SP_1760 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=170187 STRPN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</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> | + | <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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H2UR88_STRPN A0A0H2UR88_STRPN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strpn]] | + | [[Category: Streptococcus pneumoniae TIGR4]] |
| - | [[Category: Feng, Z]] | + | [[Category: Feng Z]] |
| - | [[Category: Guo, C]] | + | [[Category: Guo C]] |
| - | [[Category: Zuo, G]] | + | [[Category: Zuo G]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
A0A0H2UR88_STRPN
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
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