Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7P1H

Structure of the V. vulnificus ExoY-G-actin-profilin complex

Summary for 7P1H
Entry DOI10.2210/pdb7p1h/pdb
EMDB information13159
DescriptorMaltose/maltodextrin-binding periplasmic protein,RTX-toxin, Actin, cytoplasmic 1, Profilin-1, ... (5 entities in total)
Functional Keywordsbacterial toxin, g-actin, profilin, toxin
Biological sourceEscherichia coli (strain K12)
More
Total number of polymer chains3
Total formula weight148488.26
Authors
Belyy, A.,Merino, F.,Raunser, S. (deposition date: 2021-07-01, release date: 2021-11-17, Last modification date: 2021-12-01)
Primary citationBelyy, A.,Merino, F.,Mechold, U.,Raunser, S.
Mechanism of actin-dependent activation of nucleotidyl cyclase toxins from bacterial human pathogens.
Nat Commun, 12:6628-6628, 2021
Cited by
PubMed Abstract: 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.
PubMed: 34785651
DOI: 10.1038/s41467-021-26889-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon