6SIT
Pseudo-atomic crystal structure of the desmoglein 2 - human adenovirus serotype 3 fibre knob complex
Summary for 6SIT
| Entry DOI | 10.2210/pdb6sit/pdb |
| Related | 5erd 6qnt 6qnu |
| Descriptor | Fiber protein, Desmoglein-2, CALCIUM ION (3 entities in total) |
| Functional Keywords | virus receptor, extracellular domain, cell surface glycoprotein, desmosome, viral protein |
| Biological source | Human adenovirus B3 More |
| Total number of polymer chains | 2 |
| Total formula weight | 48120.19 |
| Authors | Burmeister, W.P.,Fender, P.,Vassal-Stermann, E. (deposition date: 2019-08-11, release date: 2019-12-18, Last modification date: 2024-01-24) |
| Primary citation | Vassal-Stermann, E.,Hutin, S.,Fender, P.,Burmeister, W.P. Intermediate-resolution crystal structure of the human adenovirus B serotype 3 fibre knob in complex with the EC2-EC3 fragment of desmoglein 2. Acta Crystallogr.,Sect.F, 75:750-757, 2019 Cited by PubMed Abstract: The cryo-electron microscopy (cryo-EM) structure of the complex between the trimeric human adenovirus B serotype 3 fibre knob and human desmoglein 2 fragments containing cadherin domains EC2 and EC3 has been published, showing 3:1 and 3:2 complexes. Here, the crystal structure determined at 4.5 Å resolution is presented with one EC2-EC3 desmoglein fragment bound per fibre knob monomer in the asymmetric unit, leading to an apparent 3:3 stoichiometry. However, in concentrated solution the 3:2 complex is predominant, as shown by small-angle X-ray scattering (SAXS), while cryo-EM at lower concentrations showed a majority of the 3:1 complex. Substitution of the calcium ions bound to the desmoglein domains by terbium ions allowed confirmation of the X-ray model using their anomalous scattering and shows that at least one binding site per cluster of calcium ions is intact and exchangeable and, combined with SAXS data, that the cadherin domains are folded even in the distal part that is invisible in the cryo-EM reconstruction. PubMed: 31797817DOI: 10.1107/S2053230X19015784 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.5 Å) |
Structure validation
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