9FGV
Cryo-EM structure of MBP homo-dimer assembled by homo Di-Gluebody
Summary for 9FGV
| Entry DOI | 10.2210/pdb9fgv/pdb |
| EMDB information | 50430 |
| Descriptor | Maltose/maltodextrin-binding periplasmic protein, Gluebody anti-MBP (2 entities in total) |
| Functional Keywords | gluebody, nanobody, cryo-em spa, small protein, protein binding |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 113829.91 |
| Authors | Yi, G.,Ye, M.,Mamalis, D.,Carrique, L.,Fairhead, M.,Li, H.,Duerr, K.,Zhang, P.,Sauer, D.B.,von Delft, F.,Davis, B.G.,Gilbert, R.J.C. (deposition date: 2024-05-26, release date: 2025-06-11, Last modification date: 2025-12-24) |
| Primary citation | Yi, G.,Mamalis, D.,Ye, M.,Carrique, L.,Fairhead, M.,Li, H.,Duerr, K.L.,Zhang, P.,Sauer, D.B.,von Delft, F.,Davis, B.G.,Gilbert, R.J.C. Covalently constrained 'Di-Gembodies' enable parallel structure solutions by cryo-EM. Nat.Chem.Biol., 2025 Cited by PubMed Abstract: Whilst cryo-electron microscopy(cryo-EM) has become a routine methodology in structural biology, obtaining high-resolution cryo-EM structures of small proteins (<100 kDa) and increasing overall throughput remain challenging. One approach to augment protein size and improve particle alignment involves the use of binding proteins or protein-based scaffolds. However, a given imaging scaffold or linking module may prove inadequate for structure solution and availability of such scaffolds remains limited. Here, we describe a strategy that exploits covalent dimerization of nanobodies to trap an engineered, predisposed nanobody-to-nanobody interface, giving Di-Gembodies as modular constructs created in homomeric and heteromeric forms. By exploiting side-chain-to-side-chain assembly, they can simultaneously display two copies of the same or two distinct proteins through a subunit interface that provides sufficient constraint required for cryo-EM structure determination. We validate this method with multiple soluble and membrane structural targets, down to 14 kDa, demonstrating a flexible and scalable platform for expanded protein structure determination. PubMed: 40817135DOI: 10.1038/s41589-025-01972-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.39 Å) |
Structure validation
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