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| | <SX load='6sgx' size='340' side='right' viewer='molstar' caption='[[6sgx]], [[Resolution|resolution]] 3.70Å' scene=''> | | <SX load='6sgx' size='340' side='right' viewer='molstar' caption='[[6sgx]], [[Resolution|resolution]] 3.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6sgx]] is a 5 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=6SGX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SGX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sgx]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SGX FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sgx OCA], [http://pdbe.org/6sgx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sgx RCSB], [http://www.ebi.ac.uk/pdbsum/6sgx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sgx ProSAT]</span></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=6sgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sgx OCA], [https://pdbe.org/6sgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sgx RCSB], [https://www.ebi.ac.uk/pdbsum/6sgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sgx 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> | + | [https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mycs2]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Famelis, N]] | + | [[Category: Famelis N]] |
| - | [[Category: Geibel, S]] | + | [[Category: Geibel S]] |
| - | [[Category: Llorca, O]] | + | [[Category: Llorca O]] |
| - | [[Category: Rivera-Calzada, A]] | + | [[Category: Rivera-Calzada A]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Type vii secretion system esx-3 secretion system t7ss esx-3 mycobacterium smegmati]]
| + | |
| Structural highlights
Function
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][1] [2]
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).
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Siegrist MS, Unnikrishnan M, McConnell MJ, Borowsky M, Cheng TY, Siddiqi N, Fortune SM, Moody DB, Rubin EJ. Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition. Proc Natl Acad Sci U S A. 2009 Nov 3;106(44):18792-7. doi:, 10.1073/pnas.0900589106. Epub 2009 Oct 21. PMID:19846780 doi:http://dx.doi.org/10.1073/pnas.0900589106
- ↑ Siegrist MS, Steigedal M, Ahmad R, Mehra A, Dragset MS, Schuster BM, Philips JA, Carr SA, Rubin EJ. Mycobacterial Esx-3 requires multiple components for iron acquisition. MBio. 2014 May 6;5(3):e01073-14. doi: 10.1128/mBio.01073-14. PMID:24803520 doi:http://dx.doi.org/10.1128/mBio.01073-14
- ↑ Famelis N, Rivera-Calzada A, Degliesposti G, Wingender M, Mietrach N, Skehel JM, Fernandez-Leiro R, Bottcher B, Schlosser A, Llorca O, Geibel S. Architecture of the mycobacterial type VII secretion system. Nature. 2019 Oct 9. pii: 10.1038/s41586-019-1633-1. doi:, 10.1038/s41586-019-1633-1. PMID:31597161 doi:http://dx.doi.org/10.1038/s41586-019-1633-1
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