View source for 8ako


==Structure of EspB-EspK complex: the non-identical twin of the PE-PPE-EspG secretion mechanism.==
<StructureSection load='8ako' size='340' side='right'caption='[[8ako]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ako]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AKO 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]] 2.293&#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=8ako FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ako OCA], [https://pdbe.org/8ako PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ako RCSB], [https://www.ebi.ac.uk/pdbsum/8ako PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ako ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ESPB_MYCTU ESPB_MYCTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogenic species from the Mycobacterium genus are responsible for a number of adverse health conditions in humans and animals that threaten health security and the economy worldwide. Mycobacteria have up to five specialized secretion systems (ESX-1 to -5) that transport virulence factors across their complex cell envelope to facilitate manipulation of their environment. In pathogenic species, these virulence factors influence the immune system's response and are responsible for membrane disruption and contributing to cell death. While structural details of these secretion systems have been recently described, gaps still remain in the structural understanding of the secretion mechanisms of most substrates. Here, we describe the crystal structure of M. tuberculosis ESX-1 secretion-associated substrate EspB bound to its chaperone EspK. We found that EspB interacts with the C-terminal domain of EspK through its helical tip. Furthermore, cryogenic electron microscopy, size exclusion chromatography analysis, and small angle X-ray scattering experiments show that EspK keeps EspB in its secretion-competent monomeric form and prevents its oligomerisation. The structure presented in this study suggests an additional secretion mechanism in ESX-1, analogous to the chaperoning of proline-glutamate (PE)-proline-proline-glutamate (PPE) proteins by EspG, where EspK facilitates the secretion of EspB in Mycobacterium species.

The crystal structure of the EspB-EspK virulence factor-chaperone complex suggests an additional type VII secretion mechanism in M. tuberculosis.,Gijsbers A, Eymery M, Gao Y, Menart I, Vinciauskaite V, Siliqi D, Peters PJ, McCarthy A, Ravelli RBG J Biol Chem. 2022 Dec 1:102761. doi: 10.1016/j.jbc.2022.102761. PMID:36463964<ref>PMID:36463964</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ako" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Eymery M]]
[[Category: Gao Y]]
[[Category: Gijsbers A]]
[[Category: Mccarthy A]]
[[Category: Menart I]]
[[Category: Peters P]]
[[Category: Ravelli RBG]]
[[Category: Siliqi D]]
[[Category: Vinciauskaite V]]