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TitleP. aeruginosa CtpA protease adopts a novel activation mechanism to initiate the proteolytic process.
Journal, issue, pagesEMBO J, Vol. 43, Issue 8, Page 1634-1652, Year 2024
Publish dateMar 11, 2024
AuthorsHao-Chi Hsu / Michelle Wang / Amanda Kovach / Andrew J Darwin / Huilin Li /
PubMed AbstractDuring bacterial cell growth, hydrolases cleave peptide cross-links between strands of the peptidoglycan sacculus to allow new strand insertion. The Pseudomonas aeruginosa carboxyl-terminal ...During bacterial cell growth, hydrolases cleave peptide cross-links between strands of the peptidoglycan sacculus to allow new strand insertion. The Pseudomonas aeruginosa carboxyl-terminal processing protease (CTP) CtpA regulates some of these hydrolases by degrading them. CtpA assembles as an inactive hexamer composed of a trimer-of-dimers, but its lipoprotein binding partner LbcA activates CtpA by an unknown mechanism. Here, we report the cryo-EM structures of the CtpA-LbcA complex. LbcA has an N-terminal adaptor domain that binds to CtpA, and a C-terminal superhelical tetratricopeptide repeat domain. One LbcA molecule attaches to each of the three vertices of a CtpA hexamer. LbcA triggers relocation of the CtpA PDZ domain, remodeling of the substrate binding pocket, and realignment of the catalytic residues. Surprisingly, only one CtpA molecule in a CtpA dimer is activated upon LbcA binding. Also, a long loop from one CtpA dimer inserts into a neighboring dimer to facilitate the proteolytic activity. This work has revealed an activation mechanism for a bacterial CTP that is strikingly different from other CTPs that have been characterized structurally.
External linksEMBO J / PubMed:38467832 / PubMed Central
MethodsEM (single particle)
Resolution3.55 - 4.14 Å
Structure data

EMDB-40846: The C-terminal protease CtpA-LbcA complex of pseudomonas aeruginosa with the TPR at the low position
Method: EM (single particle) / Resolution: 4.14 Å

EMDB-40847: The C-terminal protease CtpA-LbcA complex of pseudomonas aeruginosa with the TPR at the high position
Method: EM (single particle) / Resolution: 4.04 Å

EMDB-40848: The structure of C-terminal protease CtpA-LbcA complex of Pseudomonas aeruginosa
Method: EM (single particle) / Resolution: 3.84 Å

40849

8sxe

EMDB-40849, PDB-8sxe:
Structure of the C-terminal protease CtpA-LbcA complex of Pseudomonas aeruginosa
Method: EM (single particle) / Resolution: 3.55 Å

40850

8sxf

EMDB-40850, PDB-8sxf:
The C-terminal protease CtpA-LbcA complex of pseudomonas aeruginosa with the TPR at the high position
Method: EM (single particle) / Resolution: 3.92 Å

40851

8sxg

EMDB-40851, PDB-8sxg:
The C-terminal protease CtpA-LbcA complex of pseudomonas aeruginosa with the TPR at the low position
Method: EM (single particle) / Resolution: 4.14 Å

40852

8sxh

EMDB-40852, PDB-8sxh:
Structure of the C-terminal protease CtpA-LbcA complex of Pseudomonas aeruginosa
Method: EM (single particle) / Resolution: 3.94 Å

Source
  • pseudomonas aeruginosa (bacteria)
  • Escherichia coli (E. coli)
  • escherichia coli bl21(de3) (bacteria)
KeywordsHYDROLASE / CtpA / LbcA / C-terminal protease / pseudomonas aeruginosa

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