issue contents

ISSN: 2053-230X

October 2020 issue

Highlighted illustration

Cover illustration: Structure of the substrate-binding domain of heat-shock protein 70-x from the malaria parasite Plasmodium falciparum [Schmidt & Vakonakis (2020), Acta Cryst. F76, 495-500]. This structure supports the hypothesis that the parasite may partly exploit human chaperones for intra-erythrocytic trafficking and maintenance of its exported proteome.

research communications

link to html
The glycosomal membrane-associated Leishmania donovani protein PEX14 plays a crucial role in protein import from the cytosol to the glycosomal matrix. The carboxy-terminal coiled-coil domain, which is responsible for oligomerization, was cloned, overexpressed and purified. Crystals belonging to space group C2 and diffracting to 1.98 Å resolution were obtained from a condition containing sodium citrate at pH 7.5.

link to html
A 1.47 Å resolution crystal structure of human inositol monophosphatase bound to the inhibitor ebselen is presented. In the structure, ebselen forms a selenosulfide bond to Cys141 and ebselen-mediated contacts between two dimers give a tetramer with approximate 222 symmetry.

link to html
MacroD2, a human macrodomain protein with mono-ADP-ribosyl-hydrolyzing activity, is a single-domain protein containing a deep ADP-ribose-binding groove. Three crystal structures of human MacroD2 in the apo state, in different space groups, were determined at between 1.7 and 1.9 Å resolution. Comparison with a previous crystal structure of MacroD2 in complex with ADP-ribose revealed conformational changes in side chains, potentially facilitating design efforts of a MacroD2 inhibitor.

link to html
Protein crystallization of 3CL Mpro from SARS-CoV-2 is described along with neutron and X-ray data collection.

link to html
Crystal structure of XCC3289 (UniProt: Q8P5P7) of Xanthomonas campestris at 2.8 Å resolution is reported. The fold and spatial orientation of the two domains of XCC3289 resemble the N-terminal domains of LonA peptidases.

link to html
The 3.25 Å resolution crystallographic structure of the substrate-binding domain of the erythrocyte-exported Hsp70 chaperone from the malaria parasite Plasmodium falciparum was determined. The parasite domain is shown to be highly similar to the equivalent domain of a human Hsp70 chaperone in structure and mode of substrate engagement.

methods communications

Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds