4w4k: Difference between revisions

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New page: '''Unreleased structure''' The entry 4w4k is ON HOLD Authors: Ekiert, D.C., Cox, J.S. Description:
 
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'''Unreleased structure'''


The entry 4w4k is ON HOLD
==Crystal structure of a PE25-PPE41 heterodimer from a type VII secretion system of M. tuberculosis==
<StructureSection load='4w4k' size='340' side='right'caption='[[4w4k]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4w4k]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_str._Erdman_=_ATCC_35801 Mycobacterium tuberculosis str. Erdman = ATCC 35801]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W4K 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]] 1.95&#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=4w4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w4k OCA], [https://pdbe.org/4w4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w4k RCSB], [https://www.ebi.ac.uk/pdbsum/4w4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w4k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H3LBR3_MYCTE A0A0H3LBR3_MYCTE]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nearly 10% of the coding capacity of the Mycobacterium tuberculosis genome is devoted to two highly expanded and enigmatic protein families called PE and PPE, some of which are important virulence/immunogenicity factors and are secreted during infection via a unique alternative secretory system termed "type VII." How PE-PPE proteins function during infection and how they are translocated to the bacterial surface through the five distinct type VII secretion systems [ESAT-6 secretion system (ESX)] of M. tuberculosis is poorly understood. Here, we report the crystal structure of a PE-PPE heterodimer bound to ESX secretion-associated protein G (EspG), which adopts a novel fold. This PE-PPE-EspG complex, along with structures of two additional EspGs, suggests that EspG acts as an adaptor that recognizes specific PE-PPE protein complexes via extensive interactions with PPE domains, and delivers them to ESX machinery for secretion. Surprisingly, secretion of most PE-PPE proteins in M. tuberculosis is likely mediated by EspG from the ESX-5 system, underscoring the importance of ESX-5 in mycobacterial pathogenesis. Moreover, our results indicate that PE-PPE domains function as cis-acting targeting sequences that are read out by EspGs, revealing the molecular specificity for secretion through distinct ESX pathways.


Authors: Ekiert, D.C., Cox, J.S.
Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals molecular specificity of ESX protein secretion.,Ekiert DC, Cox JS Proc Natl Acad Sci U S A. 2014 Oct 14;111(41):14758-63. doi:, 10.1073/pnas.1409345111. Epub 2014 Oct 1. PMID:25275011<ref>PMID:25275011</ref>


Description:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4w4k" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis str. Erdman = ATCC 35801]]
[[Category: Cox JS]]
[[Category: Ekiert DC]]

Latest revision as of 07:27, 27 September 2023

Crystal structure of a PE25-PPE41 heterodimer from a type VII secretion system of M. tuberculosis

4w4k, resolution 1.95Å

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