7PH3
AMP-PNP bound nanodisc reconstituted MsbA with nanobodies, spin-labeled at position A60C
Summary for 7PH3
| Entry DOI | 10.2210/pdb7ph3/pdb |
| EMDB information | 13405 |
| Descriptor | ATP-dependent lipid A-core flippase, Nanobody Nb_MsbA#1, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (9 entities in total) |
| Functional Keywords | abc transporter, nanobody, amp-pnp, gd-dota, membrane protein |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 4 |
| Total formula weight | 161345.53 |
| Authors | Parey, K.,Januliene, D.,Galazzo, L.,Meier, G.,Vecchis, D.,Striednig, B.,Hilbi, H.,Schaefer, L.V.,Kuprov, I.,Bordignon, E.,Seeger, M.A.,Moeller, A. (deposition date: 2021-08-16, release date: 2022-08-24, Last modification date: 2024-11-06) |
| Primary citation | Galazzo, L.,Meier, G.,Januliene, D.,Parey, K.,De Vecchis, D.,Striednig, B.,Hilbi, H.,Schafer, L.V.,Kuprov, I.,Moeller, A.,Bordignon, E.,Seeger, M.A. The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells. Sci Adv, 8:eabn6845-eabn6845, 2022 Cited by PubMed Abstract: Membrane proteins are currently investigated after detergent extraction from native cellular membranes and reconstitution into artificial liposomes or nanodiscs, thereby removing them from their physiological environment. However, to truly understand the biophysical properties of membrane proteins in a physiological environment, they must be investigated within living cells. Here, we used a spin-labeled nanobody to interrogate the conformational cycle of the ABC transporter MsbA by double electron-electron resonance. Unexpectedly, the wide inward-open conformation of MsbA, commonly considered a nonphysiological state, was found to be prominently populated in cells. Molecular dynamics simulations revealed that extensive lateral portal opening is essential to provide access of its large natural substrate core lipid A to the binding cavity. Our work paves the way to investigate the conformational landscape of membrane proteins in cells. PubMed: 36223470DOI: 10.1126/sciadv.abn6845 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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