8x61
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of ATP-bound FtsE(E163Q)X== | |
| + | <StructureSection load='8x61' size='340' side='right'caption='[[8x61]], [[Resolution|resolution]] 3.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8x61]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8X61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8X61 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]] 3.05Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=8x61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8x61 OCA], [https://pdbe.org/8x61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8x61 RCSB], [https://www.ebi.ac.uk/pdbsum/8x61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8x61 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FTSE_ECOLI FTSE_ECOLI] Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring.<ref>PMID:14729705</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The peptidoglycan (PG) layer is a critical component of the bacterial cell wall and serves as an important target for antibiotics in both gram-negative and gram-positive bacteria. The hydrolysis of septal PG (sPG) is a crucial step of bacterial cell division, facilitated by FtsEX through an amidase activation system. In this study, we present the cryo-EM structures of Escherichia coli FtsEX and FtsEX-EnvC in the ATP-bound state at resolutions of 3.05 A and 3.11 A, respectively. Our PG degradation assays in E. coli reveal that the ATP-bound conformation of FtsEX activates sPG hydrolysis of EnvC-AmiB, whereas EnvC-AmiB alone exhibits autoinhibition. Structural analyses indicate that ATP binding induces conformational changes in FtsEX-EnvC, leading to significant differences from the apo state. Furthermore, PG degradation assays of AmiB mutants confirm that the regulation of AmiB by FtsEX-EnvC is achieved through the interaction between EnvC-AmiB. These findings not only provide structural insight into the mechanism of sPG hydrolysis and bacterial cell division, but also have implications for the development of novel therapeutics targeting drug-resistant bacteria. | ||
| - | + | Structure and activity of the septal peptidoglycan hydrolysis machinery crucial for bacterial cell division.,Chen Y, Gu J, Yang B, Yang L, Pang J, Luo Q, Li Y, Li D, Deng Z, Dong C, Dong H, Zhang Z PLoS Biol. 2024 May 30;22(5):e3002628. doi: 10.1371/journal.pbio.3002628. , eCollection 2024 May. PMID:38814940<ref>PMID:38814940</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8x61" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen YT]] | ||
| + | [[Category: Zhang ZY]] | ||
Current revision
Cryo-EM structure of ATP-bound FtsE(E163Q)X
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