issue contents

Journal logoSTRUCTURAL
ISSN: 2059-7983

May 2020 issue

Highlighted illustration

Cover illustration: The crystal structure of TonB-dependent transporter YncD [Grinter & Lithgow (2020), Acta Cryst. D76, 484-495]. In order to transport nutrients across their impermeable outer membrane, Gram-negative bacteria utilize a diverse family of outer-membrane proteins called TonB-dependent transporters. The majority of this family transport iron-containing substrates. However, it is becoming increasingly clear that TonB-dependent transporters target chemically diverse substrates and this article suggests that YncD is unlikely to transport an iron-containing substrate.

letters to the editor

link to html
From the perspective of a young(ish) structural biologist who currently specializes in macromolecular X-ray crystallography, are the best years of crystallography over? Some evidence and hopefully thought-provoking analysis on the subject is presented here.

research papers

link to html
The crystal and solution SAXS structures of a fragment of human leucocyte common antigen-related protein show that it is less flexible than the homologous proteins tyrosine phosphatase receptors δ and σ.

link to html
Structures of the immunodominant protein P46 from Mycoplasma hyopneumoniae have been determined by X-ray crystallography and it is shown that P46 can bind a diversity of oligosaccharides, particularly xylose, which exhibits a very high affinity for this protein. Structures of a monoclonal antibody that was raised against M. hyopnemoniae cells and specifically recognizes P46 are also reported, both alone and in complex with P46.

link to html
The bond-valence method was performed on 51 crystallographic data sets from nitrogenase proteins, indicating the presence of molybdenum(III) in FeMo cofactors and of vanadium(III) with more reduced iron complements in FeV cofactors.

link to html
Death-associated protein kinase 1 (DAPK1) was found to form a complex with purpurin and the crystal structure of the complex was determined. Purpurin may be a good lead compound for the discovery of inhibitors of DAPK1.

link to html
The apo structure of rice aldo-keto reductase has an ordered open conformation and reveals the key residues that form the substrate-channel wall and determine its substrate preference for straight-chain aldehydes.

link to html
In this work, the structure and the phylogenetic distribution of the outer-membrane transporter YncD are determined, showing that YncD is unlikely to transport an iron-containing substrate.

link to html
This paper reports the structure of Δ1-pyrroline-2-carboxylate reductase from the archaeon T. litoralis, a key enzyme in the second step of trans-4-hydroxy-L-proline metabolism that is conserved in archaea, bacteria and humans.
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds