6sgw
From Proteopedia
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<StructureSection load='6sgw' size='340' side='right'caption='[[6sgw]], [[Resolution|resolution]] 3.80Å' scene=''> | <StructureSection load='6sgw' size='340' side='right'caption='[[6sgw]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6sgw]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SGW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sgw]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SGW FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6sgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sgw OCA], [http://pdbe.org/6sgw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sgw RCSB], [http://www.ebi.ac.uk/pdbsum/6sgw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sgw ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eccB3, MSMEG_0616, MSMEI_0600 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2]), eccD3, snm, MSMEG_0623, MSMEI_0607 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2]), eccC3, MSMEG_0617, MSMEI_0601 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2]), eccE3, MSMEG_0626, MSMEI_0609 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6sgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sgw OCA], [http://pdbe.org/6sgw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sgw RCSB], [http://www.ebi.ac.uk/pdbsum/6sgw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sgw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ECCE3_MYCS2 ECCE3_MYCS2]] Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG.<ref>PMID:19846780</ref> <ref>PMID:24803520</ref> [[http://www.uniprot.org/uniprot/ECCB3_MYCS2 ECCB3_MYCS2]] An ATPase (By similarity). Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG.[UniProtKB:P9WNR7]<ref>PMID:19846780</ref> <ref>PMID:24803520</ref> [[http://www.uniprot.org/uniprot/ECCC3_MYCS2 ECCC3_MYCS2]] Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG.<ref>PMID:19846780</ref> <ref>PMID:24803520</ref> [[http://www.uniprot.org/uniprot/ECCD3_MYCS2 ECCD3_MYCS2]] Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG.<ref>PMID:19846780</ref> <ref>PMID:24803520</ref> | [[http://www.uniprot.org/uniprot/ECCE3_MYCS2 ECCE3_MYCS2]] Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG.<ref>PMID:19846780</ref> <ref>PMID:24803520</ref> [[http://www.uniprot.org/uniprot/ECCB3_MYCS2 ECCB3_MYCS2]] An ATPase (By similarity). Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG.[UniProtKB:P9WNR7]<ref>PMID:19846780</ref> <ref>PMID:24803520</ref> [[http://www.uniprot.org/uniprot/ECCC3_MYCS2 ECCC3_MYCS2]] Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG.<ref>PMID:19846780</ref> <ref>PMID:24803520</ref> [[http://www.uniprot.org/uniprot/ECCD3_MYCS2 ECCD3_MYCS2]] Part of the ESX-3 specialized secretion system, which is required for siderophore-mediated iron acquisition and for the secretion of EsxH and EsxG.<ref>PMID:19846780</ref> <ref>PMID:24803520</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Host infection by pathogenic mycobacteria such as Mycobacterium tuberculosis is facilitated by virulence factors secreted by type VII secretion systems(1). Here we report the cryo-electron microscopy structure of a membrane-embedded core complex of the ESX-3/type VII secretion system from Mycobacterium smegmatis at 3.7 A resolution. The core of the ESX-3 secretion machine consists of four protein components, EccB3:EccC3:EccD3:EccE3 in a 1:1:2:1 stoichiometry, building two identical protomers. The EccC3 coupling protein comprises a flexible array of four ATPase domains, which are linked to the membrane through a stalk domain. The 'domain of unknown function' (DUF) adjacent to the stalk is identified as an ATPase domain essential for secretion. EccB3 is predominantly periplasmatic but a small segment crosses the membrane and contacts the stalk domain, suggesting that conformational changes in the stalk domain triggered by substrate binding at the distal end of EccC3 and subsequent ATP hydrolysis in the DUF could be coupled to substrate secretion to the periplasm. Our results reveal that the architecture of type VII secretion systems differs markedly from other known secretion machines(2). | ||
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| + | Architecture of the mycobacterial type VII secretion system.,Famelis N, Rivera-Calzada A, Degliesposti G, Wingender M, Mietrach N, Skehel JM, Fernandez-Leiro R, Bottcher B, Schlosser A, Llorca O, Geibel S Nature. 2019 Oct 9. pii: 10.1038/s41586-019-1633-1. doi:, 10.1038/s41586-019-1633-1. PMID:31597161<ref>PMID:31597161</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6sgw" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Mycs2]] | ||
[[Category: Famelis, N]] | [[Category: Famelis, N]] | ||
[[Category: Geibel, S]] | [[Category: Geibel, S]] | ||
Revision as of 08:14, 23 October 2019
Structure of the ESX-3 core complex
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