8idc: Difference between revisions
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The | ==Cryo-EM structure of Mycobacterium tuberculosis FtsEX/RipC complex in peptidisc== | ||
<StructureSection load='8idc' size='340' side='right'caption='[[8idc]], [[Resolution|resolution]] 3.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8idc]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IDC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9Å</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=8idc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8idc OCA], [https://pdbe.org/8idc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8idc RCSB], [https://www.ebi.ac.uk/pdbsum/8idc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8idc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FTSE_MYCTU FTSE_MYCTU] Part of the ABC transporter FtsEX involved in cellular division. Has ATPase activity.[UniProtKB:A5U7B7][UniProtKB:P0A9R7] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The FtsEX complex regulates, directly or via a protein mediator depending on bacterial genera, peptidoglycan degradation for cell division. In mycobacteria and Gram-positive bacteria, the FtsEX system directly activates peptidoglycan-hydrolases by a mechanism that remains unclear. Here we report our investigation of Mycobacterium tuberculosis FtsEX as a non-canonical regulator with high basal ATPase activity. The cryo-EM structures of the FtsEX system alone and in complex with RipC, as well as the ATP-activated state, unveil detailed information on the signal transduction mechanism, leading to the activation of RipC. Our findings indicate that RipC is recognized through a "Match and Fit" mechanism, resulting in an asymmetric rearrangement of the extracellular domains of FtsX and a unique inclined binding mode of RipC. This study provides insights into the molecular mechanisms of FtsEX and RipC regulation in the context of a critical human pathogen, guiding the design of drugs targeting peptidoglycan remodeling. | |||
Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.,Li J, Xu X, Shi J, Hermoso JA, Sham LT, Luo M Nat Commun. 2023 Dec 4;14(1):7999. doi: 10.1038/s41467-023-43770-6. PMID:38044344<ref>PMID:38044344</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8idc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | |||
[[Category: Li J]] | |||
[[Category: Luo M]] | |||
[[Category: Xu X]] | |||
Latest revision as of 15:03, 30 October 2024
Cryo-EM structure of Mycobacterium tuberculosis FtsEX/RipC complex in peptidiscCryo-EM structure of Mycobacterium tuberculosis FtsEX/RipC complex in peptidisc
Structural highlights
FunctionFTSE_MYCTU Part of the ABC transporter FtsEX involved in cellular division. Has ATPase activity.[UniProtKB:A5U7B7][UniProtKB:P0A9R7] Publication Abstract from PubMedThe FtsEX complex regulates, directly or via a protein mediator depending on bacterial genera, peptidoglycan degradation for cell division. In mycobacteria and Gram-positive bacteria, the FtsEX system directly activates peptidoglycan-hydrolases by a mechanism that remains unclear. Here we report our investigation of Mycobacterium tuberculosis FtsEX as a non-canonical regulator with high basal ATPase activity. The cryo-EM structures of the FtsEX system alone and in complex with RipC, as well as the ATP-activated state, unveil detailed information on the signal transduction mechanism, leading to the activation of RipC. Our findings indicate that RipC is recognized through a "Match and Fit" mechanism, resulting in an asymmetric rearrangement of the extracellular domains of FtsX and a unique inclined binding mode of RipC. This study provides insights into the molecular mechanisms of FtsEX and RipC regulation in the context of a critical human pathogen, guiding the design of drugs targeting peptidoglycan remodeling. Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.,Li J, Xu X, Shi J, Hermoso JA, Sham LT, Luo M Nat Commun. 2023 Dec 4;14(1):7999. doi: 10.1038/s41467-023-43770-6. PMID:38044344[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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