forthcoming articles

E77 antibody with high binding affinity to prototype and Delta RBD was identified. The RBD/E77-Fab complex structure shows that E77 antibody mimics the binding of ACE2 to RBD and N501Y mutation from VOCs abolishes the binding potency of E77 to RBD.

A new protein structure validation method using hydrogen bonding parameters is described.

We describe the identification, characterization and X-ray structure of a novel fungal GH24 muramidase from Trichophaea saccata in which a SH3-like cell wall binding domain (CWBD) was identified by structure comparisons, in addition to its catalytic domain. A domain walking approach was then used to identify a group of fungal muramidases belonging to a new GH family, containing homologous SH3-like cell wall binding modules and we report the X-ray structures of the independent catalytic and SH3-like domains of three of them.

Raynals is an online, user-friendly, free (for academia) and advanced tool for the analysis of single-angle dynamic light scattering data. The estimation of the size distribution is done through the Tikhonov-Phillips regularization.

In this work, Martinez et al. describe the first high-resolution 3D structure of Plasmodium vivax SUB1 complexed with a substrate-derived pseudo-peptide inhibitor. Subtle conformational changes in the enzyme-inhibitor complex define new pharmacophores for iterative cycles of structure-driven synthesis to accelerate the discovery of optimized SUB1 inhibitors that could represent a new generation of anti-malarial candidates.

The first structures of C. auris dihydrofolate at near-atomic resolution are described, including apo and holo forms and complexes with two antifolate drugs: pyrimethamine and cycloguanil. C. auris is a highly significant globally emerging and resistant fungal pathogen and there is a great demand for research and progress towards novel therapeutics.

The refinement and validation of nine A-form DNA 18-mer crystal structures containing both canonical and noncanonical base pairs benefits from using dinucleotide conformational classes (NtCs).

The expression, characterization and structures of CeuE homologues from two thermophilic bacteria, G. stearothermophilus and P. thermoglucosidasius, are described together with their ligand binding. The proteins show enhanced thermostability and resistance to organic chemicals; consequently, these thermophilic homologues offer advantages in the development of artificial metalloenzymes using the CeuE family.

In this work, a novel method to recover the diffraction phase independently using the low-resolution data is proposed and it has been verified and found to be useful and practical using several typical examples. In addition, a practical metric has been established to determine whether the algorithm converges to a correct solution by estimating the entropy of the final results.

The single-component flavin-dependent tryptophan halogenase AetF converts tryptophan to 5,7-dibromotryptophan during the biosynthesis of the neurotoxin aetokthonotoxin. Crystal structures of AetF with the substrates tryptophan and 5-bromotryptophan show that a flip of the indole moiety of tryptophan positions first C5 and then C7 in the same location in the active site to facilitate two successive bromination reactions.

The crystal structure of the monocupin 5-nitrosalicylate 1,2-dioxygenase, an iron(II)-dependent ring-cleaving dioxygenase, from Bradyrhizobium sp. was determined by molecular replacement using a theoretical model obtained by AlphaFold2. Comparison with structures of other members of the same class and docking of the substrate allowed identification of the residues responsible for its very unusual enzyme selectivity.

The crystal structure of a novel laccase-like multicopper oxidase from the thermophilic fungus T. thermophila was refined at 1.9 Å resolution. Ligand-docking simulations reveal conformational changes that influence substrate specificity.

Structures of mannose 2-epimerase and a mutant from R. slithyformis were determined in their apo form and in complex with D-glucitol. In combination with a biochemical assay, the molecular basis of the substrate specificity and activity of the enzyme was elucidated.

Calixarene-mediated protein assembly provides a basis for the development of new types of biomaterials. A fourth structure of the R. solanacearum lectin–sulfonato-calix[8]arene complex expands the crystal-engineering landscape and suggests an alternative pH trigger of assembly.

It is shown that checkMySequence, an automated method for validating sequence assignment in cryo-EM structures of proteins, can be used to validate crystal structure models.