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Structure paper

TitleRegulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 7999, Year 2023
Publish dateDec 4, 2023
AuthorsJianwei Li / Xin Xu / Jian Shi / Juan A Hermoso / Lok-To Sham / Min Luo /
PubMed AbstractThe 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 ...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.
External linksNat Commun / PubMed:38044344 / PubMed Central
MethodsEM (single particle)
Resolution3.9 - 5.7 Å
Structure data

35362

8idb

EMDB-35362, PDB-8idb:
Cryo-EM structure of Mycobacterium tuberculosis FtsEX complex in peptidisc
Method: EM (single particle) / Resolution: 3.9 Å

35363

8idc

EMDB-35363, PDB-8idc:
Cryo-EM structure of Mycobacterium tuberculosis FtsEX/RipC complex in peptidisc
Method: EM (single particle) / Resolution: 3.9 Å

35364

8idd

EMDB-35364, PDB-8idd:
Cryo-EM structure of Mycobacterium tuberculosis ATP bound FtsEX/RipC complex in peptidisc
Method: EM (single particle) / Resolution: 4.0 Å

35437

8igq

EMDB-35437, PDB-8igq:
Cryo-EM structure of Mycobacterium tuberculosis ADP bound FtsEX/RipC complex in peptidisc
Method: EM (single particle) / Resolution: 5.7 Å

36304

8jia

EMDB-36304, PDB-8jia:
Cryo-EM structure of Mycobacterium tuberculosis ATP bound FtsE(E165Q)X/RipC complex in peptidisc
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsTRANSPORT PROTEIN / complex

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