Structural Biology - December 2012

Images courtesy of: Gustchina et al., PLoS Pathog., 6, e1001182, 2010;Biron et al., Biochemistry 41, 12687-12696, 2002;Tran et al., PLoS Pathog. 8, e1002797, 2012

Published: 1 December 2012

Papers selected by Alex Wlodawer

It is impossible to imagine a biochemistry journal that would not devote a significant fraction of its pages to description of macromolecular structures and, indeed, many non-structural papers also rely very much on the availability of structural data. That has not always been the case – after all, protein crystallography is just over 50 years old, it has been less than 35 years since the first protein structure was determined by NMR, and high-resolution electron microscopy applications are even more recent. However, the number of macromolecular structures deposited in the Protein Data Bank (PDB) now approaches 90,000 and other repositories contain structures obtained by NMR, electron microscopy, or molecular modelling.

FEBS Journal has been traditionally publishing many structural papers and this Virtual Issue highlights the original work published here in 2012. As special anchors we present four reviews aimed at non-specialists that describe the main techniques used in the determination of high-resolution protein structures. A vast majority of the structures presented in the original articles were solved using molecular replacement with models based on related proteins. Although these structures may not be truly novel, they are often very important, since they can elucidate enzymatic properties through analysis of inhibitor binding, compare related proteins from several species with the aim of creating selective inhibitors, or explain the biophysical properties such as thermostability or cold adaptation. Such results are crucial in both enhancing our understanding of the ways protein fold and work, as well as in practical applications such as drug design.

Some structures published here are still solved from scratch through the application of methods such as isomorphous replacement or anomalous scattering, and they represent proteins with less well studied folds. NMR was used for the determination of novel structures, for investigation of dynamic properties of macromolecules, and for elucidating intermolecular interactions. What is not shown in this Virtual Issue are many papers (actually, a fairly large fraction of all papers published in this journal) that contain figures showing protein structures that are used to interpret a variety of biological, biochemical, or biophysical data, although these papers do not report structural studies at all.

The fact that the availability of structural data is now taken completely for granted and that such structures are routinely used for interpretation of a wide range of phenomena testifies to the success of the last 50-odd years of the modern techniques of structure determination.

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