issue contents

Journal logoSTRUCTURAL
ISSN: 2059-7983

June 2020 issue

Highlighted illustration

Cover illustration: A space-filling representation of the mouse PATZ1 BTB domain structure [Piepoli et al. (2020), Acta Cryst. D76, 581-593]. PATZ1 targets the CD8 gene in lymphocyte development and interacts with the p53 protein to control genes that are important in proliferation and in the DNA-damage response. The predicted structure (in purple) of the central region was generated by homology modelling followed by conformation equilibration using molecular dynamics simulations.


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The crystal structure of DcsB, an Nω-hydroxy-L-arginine hydrolase found in the D-cycloserine biosynthetic pathway, is reported.

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Based on the structure of the N-terminal region of the S97A mutant of the stomatin operon partner protein PH1510 (1510-N), it was found that the dimeric form differs greatly from those determined previously. This result indicates that 1510-N can greatly change the form of its dimer.

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Crystal structures of the glycosyltransferase PaGT3 crystallized in the presence of crown ethers provide a basis for understanding its acceptor-recognition mechanism.


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The model-building software Buccaneer has been repurposed based on existing methods for building models into cryo-EM maps. These approaches are implemented in the latest CCP-EM model-building pipeline (version 1.4.0).

research papers

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The X-ray structure of geranylgeranylglyceryl phosphate synthase from Thermoplasma volcanium is reported, and a phylogenetic analysis and parallel ancestral state reconstruction of the evolution of the enzyme are reported for the phylum Euryarchaeota.

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Active human β-glucocerebrosidase was produced in baculovirus-transduced insect cells, purified and crystallized to yield a 0.98 Å resolution unliganded structure and a trapped covalent intermediate structure with 2-deoxy-2-fluoro-β-D-glucopyranoside.

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The crystal structures of the PATZ1 BTB domains from mammals and fish contain homodimers. The core dimer conformation of these BTB proteins is dynamically stable, despite the presence of highly flexible regions in the dimerization interface.

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Dominant inheritance of hypermethioninemia is caused by an Arg264His mutation in methionine adenosyltransferase. The mutation lowers the affinity for dimer–dimer interaction and enzymatic activity, which can be restored by chemical intervention.


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An obituary is published for Jean-Luc Ferrer, an internationally known and highly respected scientist in protein crystallography, whose work led to many innovative instrumental and methodological developments in structural biology.
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