View source for 8gmh


==Crystal Structure of the ternary complex of TelA-LXG, LapA3, and LapA4==
<StructureSection load='8gmh' size='340' side='right'caption='[[8gmh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8gmh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_intermedius_B196 Streptococcus intermedius B196]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GMH 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=8gmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gmh OCA], [https://pdbe.org/8gmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gmh RCSB], [https://www.ebi.ac.uk/pdbsum/8gmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gmh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/T1ZCZ9_STRIT T1ZCZ9_STRIT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Type VII secretion systems are membrane-embedded nanomachines used by Gram-positive bacteria to export effector proteins from the cytoplasm to the extracellular environment. Many of these effectors are polymorphic toxins comprised of an N-terminal Leu-x-Gly (LXG) domain of unknown function and a C-terminal toxin domain that inhibits the growth of bacterial competitors. In recent work, it was shown that LXG effectors require two cognate Lap proteins for T7SS-dependent export. Here, we present the 2.6 A structure of the LXG domain of the TelA toxin from the opportunistic pathogen Streptococcus intermedius in complex with both of its cognate Lap targeting factors. The structure reveals an elongated alpha-helical bundle within which each Lap protein makes extensive hydrophobic contacts with either end of the LXG domain. Remarkably, despite low overall sequence identity, we identify striking structural similarity between our LXG complex and PE-PPE heterodimers exported by the distantly related ESX type VII secretion systems of Mycobacteria implying a conserved mechanism of effector export among diverse Gram-positive bacteria. Overall, our findings demonstrate that LXG domains, in conjunction with their cognate Lap targeting factors, represent a tripartite secretion signal for a widespread family of T7SS toxins.

Structure of a tripartite protein complex that targets toxins to the type VII secretion system.,Klein TA, Shah PY, Gkragkopoulou P, Grebenc DW, Kim Y, Whitney JC Proc Natl Acad Sci U S A. 2024 Jan 16;121(3):e2312455121. doi: , 10.1073/pnas.2312455121. Epub 2024 Jan 9. PMID:38194450<ref>PMID:38194450</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8gmh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus intermedius B196]]
[[Category: Gkragkopoulou P]]
[[Category: Grebenc DW]]
[[Category: Kim Y]]
[[Category: Klein TA]]
[[Category: Shah PY]]
[[Category: Whitney JC]]