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Intermediate‐resolution crystal structure of the human adenovirus B serotype 3 fibre knob in complex with the EC2‐EC3 fragment of desmoglein 2
Author(s) -
Vassal-Stermann Emilie,
Hutin Stephanie,
Fender Pascal,
Burmeister Wim P.
Publication year - 2019
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x19015784
Subject(s) - crystallography , small angle x ray scattering , anomalous scattering , desmoglein , chemistry , resolution (logic) , crystal structure , scattering , physics , optics , cadherin , biochemistry , artificial intelligence , computer science , cell
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.