5YUD
Flagellin derivative in complex with the NLR protein NAIP5
Summary for 5YUD
| Entry DOI | 10.2210/pdb5yud/pdb |
| EMDB information | 6845 |
| Descriptor | Baculoviral IAP repeat-containing protein 1e, Phase 2 flagellin,Flagellin, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | flagellin, naip5, nlrc4, cryo-em, immune system |
| Biological source | Mus musculus (Mouse) More |
| Cellular location | Secreted: P06179 |
| Total number of polymer chains | 2 |
| Total formula weight | 168190.59 |
| Authors | Yang, X.R.,Yang, F.,Wang, W.G.,Lin, G.Z. (deposition date: 2017-11-21, release date: 2018-01-03, Last modification date: 2024-03-27) |
| Primary citation | Yang, X.,Yang, F.,Wang, W.,Lin, G.,Hu, Z.,Han, Z.,Qi, Y.,Zhang, L.,Wang, J.,Sui, S.F.,Chai, J. Structural basis for specific flagellin recognition by the NLR protein NAIP5. Cell Res., 28:35-47, 2018 Cited by PubMed Abstract: The nucleotide-binding domain- and leucine-rich repeat (LRR)-containing proteins (NLRs) function as intracellular immune receptors to detect the presence of pathogen- or host-derived signals. The mechanisms of how NLRs sense their ligands remain elusive. Here we report the structure of a bacterial flagellin derivative in complex with the NLR proteins NAIP5 and NLRC4 determined by cryo-electron microscopy at 4.28 Å resolution. The structure revealed that the flagellin derivative forms two parallel helices interacting with multiple domains including BIR1 and LRR of NAIP5. Binding to NAIP5 results in a nearly complete burial of the flagellin derivative, thus stabilizing the active conformation of NAIP5. The extreme C-terminal side of the flagellin is anchored to a sterically constrained binding pocket of NAIP5, which likely acts as a structural determinant for discrimination of different bacterial flagellins by NAIP5, a notion further supported by biochemical data. Taken together, our results shed light on the molecular mechanisms underlying NLR ligand perception. PubMed: 29182158DOI: 10.1038/cr.2017.148 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.28 Å) |
Structure validation
Download full validation report
