How the Protein Data Bank changed biology: An introduction to the JBC Reviews thematic series, part 1

Helen M Berman,Lila M Gierasch

doi:10.1016/j.jbc.2021.100608

Abstract

This collection of articles celebrates the 50th anniversary of the Protein Data Bank (PDB), the single global digital archive of biological macromolecular structures. The impact of the PDB is immense; we have invited a number of top researchers in structural biology to illustrate its influence on an array of scientific fields. What emerges is a compelling picture of the synergism between the PDB and the explosive progress witnessed in many scientific areas. Availability of reliable, openly accessible, well-archived structural information has arguably had more impact on cell and molecular biology than even some of the enabling technologies such as PCR. We have seen the science move from a time when structural biologists contributed the lion’s share of the structures to the PDB and for discussion within their community to a time when any effort to achieve in-depth understanding of a biochemical or cell biological question demands an interdisciplinary approach built atop structural underpinnings.

Highlights

TO THEMATIC SERIES: Celebrating the science to present this collection to you, as JBC has taken center stage in the history of the Protein Data Bank (PDB) for two key reasons: First, JBC was one of the first journals to require that authors deposit structural data reported in accepted articles to the PDB (4)
The structures in the PDB are diverse in almost every respect and cover multiple areas of biology and biochemistry
Part 2 will include more reviews that celebrate additional scientific areas that have been profoundly touched by the creation of the PDB

Summary

Introduction

He points out the challenges that those first ribosome structures presented for the PDB. Moore’s review captures the transition from reliance on X-ray crystallography to study these large machines to the current practice of using 3D electron microscopy for most ribosome structures, and why that is the method of choice for these large assemblies.

Results

Conclusion