7F3N
Structure of PopP2 in apo form
Summary for 7F3N
| Entry DOI | 10.2210/pdb7f3n/pdb |
| Descriptor | Type III effector protein popp2 (2 entities in total) |
| Functional Keywords | yopj, popp2, acetyltransferase, transferase |
| Biological source | Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum) |
| Total number of polymer chains | 1 |
| Total formula weight | 37738.67 |
| Authors | Xia, Y.,Zhang, Z.M. (deposition date: 2021-06-16, release date: 2021-11-17, Last modification date: 2023-11-29) |
| Primary citation | Xia, Y.,Zou, R.,Escouboue, M.,Zhong, L.,Zhu, C.,Pouzet, C.,Wu, X.,Wang, Y.,Lv, G.,Zhou, H.,Sun, P.,Ding, K.,Deslandes, L.,Yuan, S.,Zhang, Z.M. Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase. Nat Commun, 12:5969-5969, 2021 Cited by PubMed Abstract: The Yersinia outer protein J (YopJ) family effectors are widely deployed through the type III secretion system by both plant and animal pathogens. As non-canonical acetyltransferases, the enzymatic activities of YopJ family effectors are allosterically activated by the eukaryote-specific ligand inositol hexaphosphate (InsP6). However, the underpinning molecular mechanism remains undefined. Here we present the crystal structure of apo-PopP2, a YopJ family member secreted by the plant pathogen Ralstonia solanacearum. Structural comparison of apo-PopP2 with the InsP6-bound PopP2 reveals a substantial conformational readjustment centered in the substrate-binding site. Combining biochemical and computational analyses, we further identify a mechanism by which the association of InsP6 with PopP2 induces an α-helix-to-β-strand transition in the catalytic core, resulting in stabilization of the substrate recognition helix in the target protein binding site. Together, our study uncovers the molecular basis governing InsP6-mediated allosteric regulation of YopJ family acetyltransferases and further expands the paradigm of fold-switching proteins. PubMed: 34645811DOI: 10.1038/s41467-021-26183-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35185590332 Å) |
Structure validation
Download full validation report
