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TitleMechanism of actin-dependent activation of nucleotidyl cyclase toxins from bacterial human pathogens.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 6628, Year 2021
Publish dateNov 16, 2021
AuthorsAlexander Belyy / Felipe Merino / Undine Mechold / Stefan Raunser /
PubMed AbstractBacterial human pathogens secrete initially inactive nucleotidyl cyclases that become potent enzymes by binding to actin inside eukaryotic host cells. The underlying molecular mechanism of this ...Bacterial human pathogens secrete initially inactive nucleotidyl cyclases that become potent enzymes by binding to actin inside eukaryotic host cells. The underlying molecular mechanism of this activation is, however, unclear. Here, we report structures of ExoY from Pseudomonas aeruginosa and Vibrio vulnificus bound to their corresponding activators F-actin and profilin-G-actin. The structures reveal that in contrast to the apo-state, two flexible regions become ordered and interact strongly with actin. The specific stabilization of these regions results in an allosteric stabilization of the nucleotide binding pocket and thereby to an activation of the enzyme. Differences in the sequence and conformation of the actin-binding regions are responsible for the selective binding to either F- or G-actin. Other nucleotidyl cyclase toxins that bind to calmodulin rather than actin undergo a similar disordered-to-ordered transition during activation, suggesting that the allosteric activation-by-stabilization mechanism of ExoY is conserved in these enzymes, albeit the different activator.
External linksNat Commun / PubMed:34785651 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.2 Å
Structure data

13158

7p1g

EMDB-13158, PDB-7p1g:
Structure of the P. aeruginosa ExoY-F-actin complex
Method: EM (single particle) / Resolution: 3.2 Å

13159

7p1h

EMDB-13159, PDB-7p1h:
Structure of the V. vulnificus ExoY-G-actin-profilin complex
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-13160:
V. nigripulchritudo ExoY-G-actin-complex
Method: EM (single particle) / Resolution: 4.2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-GH3:
3'-DEOXY-GUANOSINE-5'-TRIPHOSPHATE

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

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-CA:
Unknown entry

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

Source
  • pseudomonas aeruginosa pao1 (bacteria)
  • Rabbit (rabbit)
  • amanita phalloides (death cap)
  • vibrio vulnificus (bacteria)
  • homo sapiens (human)
  • Vibrio nigripulchritudo (bacteria)
  • oryctolagus cuniculus (rabbit)
  • escherichia coli k-12 (bacteria)
  • escherichia coli (strain k12) (bacteria)
KeywordsTOXIN / Bacterial toxin / F-actin / G-actin / profilin

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