7OMM
Cryo-EM structure of N. gonorhoeae LptDE in complex with ProMacrobodies (MBPs have not been built de novo)
Summary for 7OMM
| Entry DOI | 10.2210/pdb7omm/pdb |
| EMDB information | 12990 |
| Descriptor | LPS-assembly protein LptD, LPS-assembly lipoprotein LptE, ProMacrobody 21,Maltodextrin-binding protein, ... (4 entities in total) |
| Functional Keywords | outer membrane protein lps transporter bacterial transporter neisseria gonorrhoeae drug target promacrobodies structural chaperone cryo-electron microscopy, transport protein |
| Biological source | Neisseria gonorrhoeae More |
| Total number of polymer chains | 4 |
| Total formula weight | 219732.04 |
| Authors | Botte, M.,Ni, D.,Schenck, S.,Zimmermann, I.,Chami, M.,Bocquet, N.,Egloff, P.,Bucher, D.,Trabuco, M.,Cheng, R.K.Y.,Brunner, J.D.,Seeger, M.A.,Stahlberg, H.,Hennig, M. (deposition date: 2021-05-24, release date: 2022-05-04, Last modification date: 2024-10-23) |
| Primary citation | Botte, M.,Ni, D.,Schenck, S.,Zimmermann, I.,Chami, M.,Bocquet, N.,Egloff, P.,Bucher, D.,Trabuco, M.,Cheng, R.K.Y.,Brunner, J.D.,Seeger, M.A.,Stahlberg, H.,Hennig, M. Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation. Nat Commun, 13:1826-1826, 2022 Cited by PubMed Abstract: Lipopolysaccharides are major constituents of the extracellular leaflet in the bacterial outer membrane and form an effective physical barrier for environmental threats and for antibiotics in Gram-negative bacteria. The last step of LPS insertion via the Lpt pathway is mediated by the LptD/E protein complex. Detailed insights into the architecture of LptDE transporter complexes have been derived from X-ray crystallography. However, no structure of a laterally open LptD transporter, a transient state that occurs during LPS release, is available to date. Here, we report a cryo-EM structure of a partially opened LptDE transporter in complex with rigid chaperones derived from nanobodies, at 3.4 Å resolution. In addition, a subset of particles allows to model a structure of a laterally fully opened LptDE complex. Our work offers insights into the mechanism of LPS insertion, provides a structural framework for the development of antibiotics targeting LptD and describes a highly rigid chaperone scaffold to enable structural biology of challenging protein targets. PubMed: 35383177DOI: 10.1038/s41467-022-29459-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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