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PDB 50th anniversary: celebrating the future of structural biology
In honour of the 50th anniversary of the Protein Data Bank, we and our colleagues at Nature Methodspresent a special online Collection that celebrates the past and future of structural biology.
Image: Cross-section through a B-cell showing release of antibodies. Illustration by David S. Goodsell, The Machinery of Life, published 2009 by Springer Nature. Cover Design: Bethany Vukomanovic.
We celebrate the 50th anniversary of the Protein Data Bank together with our colleagues at Nature Methods with a special collection that showcases key achievements in structural biology and views of its future.
The Protein Data Bank (PDB) is a community resource. But how do we define community, and how has it changed over the last 50 years since the PDB was founded? How did the community influence the evolution of the PDB, and how did the PDB influence both the science and the behavior of the community?
Artistic techniques are essential tools to visualize, understand and disseminate the results of scientific research. The field of structural biology has enjoyed a particularly productive marriage of art and science.
Structural biology plays a crucial role in the fight against COVID-19, permitting us to ‘see’ and understand SARS-CoV-2. However, the macromolecular structures of SARS-CoV-2 proteins that were solved with great speed and urgency can contain errors that may hinder drug design. The Coronavirus Structural Task Force has been working behind the scenes to evaluate and improve these structures, making the results freely available at https://insidecorona.net/.
The biogenesis of eukaryotic 20S proteasomes requires the accurate assembly of 14 closely related protein subunits and occurs in a complex series of chaperone-dependent steps. Important insights into this pathway are now provided by the high-resolution cryo-EM structures of two 20S proteasome assembly intermediates.
The cryo-EM structure of DNA-assembled histone pairs Hβ-Hα and Hδ-Hγ from Marseillevirus, a nucleocytoplasmic large DNA virus, reveals that these proteins form viral nucleosomes with highly conserved features when compared to canonical eukaryotic nucleosomes.
Cryo-EM structures of assembly intermediates of the proteasome 20S core particle show how the coordinated activity of chaperones orchestrates early steps in proteasome biogenesis.
Structural and functional characterization of two neutralizing antibodies that target conserved, nonoverlapping epitopes in HeV and NiV F protein trimers and inhibit membrane fusion establishes the therapeutic potential of antibody cocktails to protect against henipavirus infection.
The histone variant H2A.Z.1 influences the rate of RNAPII pause release and controls re-loading of TFIIB and TBP at promoters to ensure proper induction of gene expression programs.
Structural elucidation and functional analysis of the human GMPPA–GMPPB complex reveals how GMPPA acts as a ‘sensor’ of GDP-mannose to allosterically regulate GMPPB activity.