8igq: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8igq is ON HOLD
+==Cryo-EM structure of Mycobacterium tuberculosis ADP bound FtsEX/RipC complex in peptidisc==
+<StructureSection load='8igq' size='340' side='right'caption='[[8igq]], [[Resolution|resolution]] 5.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8igq]] 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=8IGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IGQ 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]] 5.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></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=8igq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8igq OCA], [https://pdbe.org/8igq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8igq RCSB], [https://www.ebi.ac.uk/pdbsum/8igq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8igq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Y2190_MYCTU Y2190_MYCTU]
+<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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8igq" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mycobacterium tuberculosis]]
+[[Category: Li J]]
+[[Category: Luo M]]
+[[Category: Xu X]]