7Z7I
Structure of ADP-ribosylated F-actin
Summary for 7Z7I
| Entry DOI | 10.2210/pdb7z7i/pdb |
| EMDB information | 14533 |
| Descriptor | Actin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | f-actin, cytosolic protein |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 5 |
| Total formula weight | 215603.97 |
| Authors | Belyy, A.,Raunser, S. (deposition date: 2022-03-15, release date: 2022-06-29, Last modification date: 2023-03-15) |
| Primary citation | Belyy, A.,Lindemann, F.,Roderer, D.,Funk, J.,Bardiaux, B.,Protze, J.,Bieling, P.,Oschkinat, H.,Raunser, S. Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin. Nat Commun, 13:4202-4202, 2022 Cited by PubMed Abstract: Tc toxins deliver toxic enzymes into host cells by a unique injection mechanism. One of these enzymes is the actin ADP-ribosyltransferase TccC3, whose activity leads to the clustering of the cellular cytoskeleton and ultimately cell death. Here, we show in atomic detail how TccC3 modifies actin. We find that the ADP-ribosyltransferase does not bind to G-actin but interacts with two consecutive actin subunits of F-actin. The binding of TccC3 to F-actin occurs via an induced-fit mechanism that facilitates access of NAD to the nucleotide binding pocket. The following nucleophilic substitution reaction results in the transfer of ADP-ribose to threonine-148 of F-actin. We demonstrate that this site-specific modification of F-actin prevents its interaction with depolymerization factors, such as cofilin, which impairs actin network turnover and leads to steady actin polymerization. Our findings reveal in atomic detail a mechanism of action of a bacterial toxin through specific targeting and modification of F-actin. PubMed: 35858890DOI: 10.1038/s41467-022-31836-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
Download full validation report
