issue contents
January 2017 issue
research communications
Selective targeting of the ζ1 subunit of the human coatomer protein complex I (Copζ1) is a promising avenue for anticancer therapy, as knockouts of ζ1 have been shown to specifically kill both proliferating and nondividing tumour-cell populations. In order to provide a structural basis for rational drug design, the high-resolution crystal structure of Copζ1 is reported.
PDB reference: Copζ1, 5mc7
The C-terminal domain (residues 780–1122) of the ATPase motor Fun30 from S. cerevisiae has been crystallized and the structure was determined at a resolution of 1.95 Å. A helix-bundle insertion in the ATPase domain was identified to be specific to the Fun30 subfamily.
PDB reference: C-terminal part of Fun30 ATPase domain, 5gn1
The crystal structure of an IclR homologue from Microbacterium sp. strain HM58-2 was determined at 2.1 Å resolution. It revealed a unique tetramer conformation, which may represent one of the multiple conformations in transcriptional regulation.
PDB reference: Mi-IclR, 5h1a
The crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC has been determined to a nominal resolution of 2.95 Å.
PDB reference: malonate semialdehyde dehydrogenase, 5tjr
The crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC has been determined to a resolution of 2.07 Å.
PDB reference: putrescine aminotransferase, 5ti8
The structure of a new fungal form of aspartate-semialdehyde dehydrogenase from A. fumigatus reveals differences in secondary-structural features that will be exploited for species-selective antibiotic development.
PDB reference: A. fumigatus ASADH, 5jw6
The extracellular domain of human hepatocyte growth factor activator inhibitor 1 was expressed in Drosophila S2 cells. The recombinant protein was crystallized using ammonium sulfate as precipitant and the crystals diffracted to 3.8 Å resolution, with unit-cell parameters a = b = 95.42, c = 124.50 Å.
To explore the sequence–structure relationships of four-α-helical bundles, the revRM6 protein, which has been engineered with the exact inverse amino-acid sequence of a hyperthermophilic helical bundle, was expressed, purified and crystallized and X-ray diffraction data were collected.
Open access
The crystal structure of SP0092 was determined at 1.61 Å resolution and reveals a domain-swapped dimer with the monomer subunit in a closed conformation in the absence of ligand.
PDB reference: SP0092, 5mlt