7r49
From Proteopedia
(Difference between revisions)
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- | ==== | + | ==Crystal structure of the L. plantarum acyl carrier protein synthase (AcpS)in complex with D-alanyl carrier protein (DltC1)== |
- | <StructureSection load='7r49' size='340' side='right'caption='[[7r49]]' scene=''> | + | <StructureSection load='7r49' size='340' side='right'caption='[[7r49]], [[Resolution|resolution]] 1.88Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7r49]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactiplantibacillus_plantarum_subsp._plantarum_NC8 Lactiplantibacillus plantarum subsp. plantarum NC8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R49 FirstGlance]. <br> |
- | </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=7r49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r49 OCA], [https://pdbe.org/7r49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r49 RCSB], [https://www.ebi.ac.uk/pdbsum/7r49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r49 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=7r49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r49 OCA], [https://pdbe.org/7r49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r49 RCSB], [https://www.ebi.ac.uk/pdbsum/7r49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r49 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[https://www.uniprot.org/uniprot/ACPS_LACPL ACPS_LACPL]] Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Teichoic acids (TA) are crucial for the homeostasis of the bacterial cell wall as well as their developmental behavior and interplay with the environment. TA can be decorated by different modifications, modulating thus their biochemical properties. One major modification consists in the esterification of TA by D-alanine, a process known as D-alanylation. TA D-alanylation is performed by the Dlt pathway, which starts in the cytoplasm and continues extracellularly after D-Ala transportation through the membrane. In this study, we combined structural biology and in vivo approaches to dissect the cytoplasmic steps of this pathway in Lactiplantibacillus plantarum, a bacterial species conferring health benefits to its animal host. After establishing that AcpS, DltB, DltC1 and DltA are required for the promotion of Drosophila juvenile growth under chronic undernutrition, we solved their crystal structure and/or used NMR and molecular modeling to study their interactions. Our work demonstrates that the suite of interactions between these proteins is ordered with a conserved surface of DltC1 docking sequentially AcpS, DltA and eventually DltB. Altogether, we conclude that DltC1 acts as an interaction hub for all the successive cytoplasmic steps of the TA D-alanylation pathway. | ||
+ | |||
+ | DltC acts as an interaction hub for AcpS, DltA and DltB in the teichoic acid D-alanylation pathway of Lactiplantibacillus plantarum.,Nikolopoulos N, Matos RC, Courtin P, Ayala I, Akherraz H, Simorre JP, Chapot-Chartier MP, Leulier F, Ravaud S, Grangeasse C Sci Rep. 2022 Jul 30;12(1):13133. doi: 10.1038/s41598-022-17434-2. PMID:35907949<ref>PMID:35907949</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7r49" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Lactiplantibacillus plantarum subsp. plantarum NC8]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Grangeasse C]] |
+ | [[Category: Nikolopoulos N]] | ||
+ | [[Category: Ravaud S]] | ||
+ | [[Category: Simorre JP]] |
Revision as of 03:12, 8 September 2022
Crystal structure of the L. plantarum acyl carrier protein synthase (AcpS)in complex with D-alanyl carrier protein (DltC1)
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