8OI3
Structure of NopD with AtSUMO2
Summary for 8OI3
| Entry DOI | 10.2210/pdb8oi3/pdb |
| Descriptor | Type III effector, Small ubiquitin-related modifier 2, prop-2-en-1-amine, ... (4 entities in total) |
| Functional Keywords | sumo protease, complex, plant sumo2, hydrolase |
| Biological source | Bradyrhizobium More |
| Total number of polymer chains | 4 |
| Total formula weight | 67973.81 |
| Authors | Reverter, D.,Li, Y. (deposition date: 2023-03-22, release date: 2024-04-03, Last modification date: 2024-10-16) |
| Primary citation | Li, Y.,Perez-Gil, J.,Lois, L.M.,Varejao, N.,Reverter, D. Broad-spectrum ubiquitin/ubiquitin-like deconjugation activity of the rhizobial effector NopD from Bradyrhizobium (sp. XS1150). Commun Biol, 7:644-644, 2024 Cited by PubMed Abstract: The post-translational modification of proteins by ubiquitin-like modifiers (UbLs), such as SUMO, ubiquitin, and Nedd8, regulates a vast array of cellular processes. Dedicated UbL deconjugating proteases families reverse these modifications. During bacterial infection, effector proteins, including deconjugating proteases, are released to disrupt host cell defenses and promote bacterial survival. NopD, an effector protein from rhizobia involved in legume nodule symbiosis, exhibits deSUMOylation activity and, unexpectedly, also deubiquitination and deNeddylation activities. Here, we present two crystal structures of Bradyrhizobium (sp. XS1150) NopD complexed with either Arabidopsis SUMO2 or ubiquitin at 1.50 Å and 1.94 Å resolution, respectively. Despite their low sequence similarity, SUMO and ubiquitin bind to a similar NopD interface, employing a unique loop insertion in the NopD sequence. In vitro binding and activity assays reveal specific residues that distinguish between deubiquitination and deSUMOylation. These unique multifaceted deconjugating activities against SUMO, ubiquitin, and Nedd8 exemplify an optimized bacterial protease that disrupts distinct UbL post-translational modifications during host cell infection. PubMed: 38802699DOI: 10.1038/s42003-024-06344-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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