7b7j: Difference between revisions
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==EccD5 ubiqutin like domain from Mycobacterium xenopi== | ==EccD5 ubiqutin like domain from Mycobacterium xenopi== | ||
<StructureSection load='7b7j' size='340' side='right'caption='[[7b7j]]' scene=''> | <StructureSection load='7b7j' size='340' side='right'caption='[[7b7j]], [[Resolution|resolution]] 1.66Å' 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=7B7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B7J FirstGlance]. <br> | <table><tr><td colspan='2'>[[7b7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_xenopi Mycobacterium xenopi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B7J 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=7b7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b7j OCA], [https://pdbe.org/7b7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b7j RCSB], [https://www.ebi.ac.uk/pdbsum/7b7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b7j ProSAT]</span></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]] 1.66Å</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=7b7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b7j OCA], [https://pdbe.org/7b7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b7j RCSB], [https://www.ebi.ac.uk/pdbsum/7b7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b7j ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/I0RSS8_MYCXE I0RSS8_MYCXE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ESX-5 type VII secretion system is a membrane-spanning protein complex key to the virulence of mycobacterial pathogens. However, the overall architecture of the fully assembled translocation machinery and the composition of the central secretion pore have remained unknown. Here, we present the high-resolution structure of the 2.1-megadalton ESX-5 core complex. Our structure captured a dynamic, secretion-competent conformation of the pore within a well-defined transmembrane section, sandwiched between two flexible protein layers at the cytosolic entrance and the periplasmic exit. We propose that this flexibility endows the ESX-5 machinery with large conformational plasticity required to accommodate targeted protein secretion. Compared to known secretion systems, a highly dynamic state of the pore may represent a fundamental principle of bacterial secretion machineries. | |||
Structure of the mycobacterial ESX-5 type VII secretion system pore complex.,Beckham KSH, Ritter C, Chojnowski G, Ziemianowicz DS, Mullapudi E, Rettel M, Savitski MM, Mortensen SA, Kosinski J, Wilmanns M Sci Adv. 2021 Jun 25;7(26). pii: 7/26/eabg9923. doi: 10.1126/sciadv.abg9923., Print 2021 Jun. PMID:34172453<ref>PMID:34172453</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7b7j" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mycobacterium xenopi]] | |||
[[Category: Beckham KS]] | [[Category: Beckham KS]] | ||
[[Category: Wilmanns M]] | [[Category: Wilmanns M]] | ||
Latest revision as of 15:23, 1 February 2024
EccD5 ubiqutin like domain from Mycobacterium xenopiEccD5 ubiqutin like domain from Mycobacterium xenopi
Structural highlights
FunctionPublication Abstract from PubMedThe ESX-5 type VII secretion system is a membrane-spanning protein complex key to the virulence of mycobacterial pathogens. However, the overall architecture of the fully assembled translocation machinery and the composition of the central secretion pore have remained unknown. Here, we present the high-resolution structure of the 2.1-megadalton ESX-5 core complex. Our structure captured a dynamic, secretion-competent conformation of the pore within a well-defined transmembrane section, sandwiched between two flexible protein layers at the cytosolic entrance and the periplasmic exit. We propose that this flexibility endows the ESX-5 machinery with large conformational plasticity required to accommodate targeted protein secretion. Compared to known secretion systems, a highly dynamic state of the pore may represent a fundamental principle of bacterial secretion machineries. Structure of the mycobacterial ESX-5 type VII secretion system pore complex.,Beckham KSH, Ritter C, Chojnowski G, Ziemianowicz DS, Mullapudi E, Rettel M, Savitski MM, Mortensen SA, Kosinski J, Wilmanns M Sci Adv. 2021 Jun 25;7(26). pii: 7/26/eabg9923. doi: 10.1126/sciadv.abg9923., Print 2021 Jun. PMID:34172453[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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