7cu9: Difference between revisions
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==Crystal structure of the soluble domain of TiME protein from Mycobacterium smegmatis== | ==Crystal structure of the soluble domain of TiME protein from Mycobacterium smegmatis== | ||
<StructureSection load='7cu9' size='340' side='right'caption='[[7cu9]]' scene=''> | <StructureSection load='7cu9' size='340' side='right'caption='[[7cu9]], [[Resolution|resolution]] 1.55Å' 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=7CU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CU9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7cu9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CU9 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=7cu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cu9 OCA], [https://pdbe.org/7cu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cu9 RCSB], [https://www.ebi.ac.uk/pdbsum/7cu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cu9 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_6251 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7cu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cu9 OCA], [https://pdbe.org/7cu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cu9 RCSB], [https://www.ebi.ac.uk/pdbsum/7cu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cu9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Tuberculosis-causing mycobacteria have thick cell-wall and capsule layers that are formed from complex structures. Protein secretion across these barriers depends on a specialized protein secretion system, but none has been reported. We show that Mycobacterium tuberculosis Rv3705c and its homologous MSMEG_6251 in Mycobacterium smegmatis are tube-forming proteins in the mycobacterial envelope (TiME). Crystallographic and cryo-EM structures of these two proteins show that both proteins form rotationally symmetric rings. Two layers of TiME rings pack together in a tail-to-tail manner into a ring-shaped complex, which, in turn, stacks together to form tubes. M. smegmatis TiME was detected mainly in the cell wall and capsule. Knocking out the TiME gene markedly decreased the amount of secreted protein in the M. smegmatis culture medium, and expression of this gene in knocked-out strain partially restored the level of secreted protein. Our structure and functional data thus suggest that TiME forms a protein transport tube across the mycobacterial outer envelope. | |||
Identification and architecture of a putative secretion tube across mycobacterial outer envelope.,Cai X, Liu L, Qiu C, Wen C, He Y, Cui Y, Li S, Zhang X, Zhang L, Tian C, Bi L, Zhou ZH, Gong W Sci Adv. 2021 Aug 20;7(34). pii: 7/34/eabg5656. doi: 10.1126/sciadv.abg5656., Print 2021 Aug. PMID:34417177<ref>PMID:34417177</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7cu9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cai X]] | [[Category: Mycs2]] | ||
[[Category: Gong W]] | [[Category: Cai, X]] | ||
[[Category: Liu L]] | [[Category: Gong, W]] | ||
[[Category: Wen C]] | [[Category: Liu, L]] | ||
[[Category: Wen, C]] | |||
[[Category: Envelope-spanning channel]] | |||
[[Category: Potential drug target]] | |||
[[Category: Protein transport]] | |||
[[Category: Tubular protein]] | |||
Revision as of 10:13, 16 March 2022
Crystal structure of the soluble domain of TiME protein from Mycobacterium smegmatisCrystal structure of the soluble domain of TiME protein from Mycobacterium smegmatis
Structural highlights
Publication Abstract from PubMedTuberculosis-causing mycobacteria have thick cell-wall and capsule layers that are formed from complex structures. Protein secretion across these barriers depends on a specialized protein secretion system, but none has been reported. We show that Mycobacterium tuberculosis Rv3705c and its homologous MSMEG_6251 in Mycobacterium smegmatis are tube-forming proteins in the mycobacterial envelope (TiME). Crystallographic and cryo-EM structures of these two proteins show that both proteins form rotationally symmetric rings. Two layers of TiME rings pack together in a tail-to-tail manner into a ring-shaped complex, which, in turn, stacks together to form tubes. M. smegmatis TiME was detected mainly in the cell wall and capsule. Knocking out the TiME gene markedly decreased the amount of secreted protein in the M. smegmatis culture medium, and expression of this gene in knocked-out strain partially restored the level of secreted protein. Our structure and functional data thus suggest that TiME forms a protein transport tube across the mycobacterial outer envelope. Identification and architecture of a putative secretion tube across mycobacterial outer envelope.,Cai X, Liu L, Qiu C, Wen C, He Y, Cui Y, Li S, Zhang X, Zhang L, Tian C, Bi L, Zhou ZH, Gong W Sci Adv. 2021 Aug 20;7(34). pii: 7/34/eabg5656. doi: 10.1126/sciadv.abg5656., Print 2021 Aug. PMID:34417177[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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