Using resources generated by the Seattle Structural Genomics Center for Infectious Disease (SSGCID) for training early career researchers

The focused issue on Empowering education through structural genomics is introduced. The virtual issue is available at https://journals.iucr.org/special_issues/2024/educationsg.

Crystal structures of the putative endoribonuclease L-PSP from Entamoeba histolytica

The purification, crystallization and three crystal structures of the putative endoribonuclease L-PSP from E. histolytica are reported.

Structure of an Fe²⁺-binding-deficient mimiviral collagen lysyl hydroxylase

Fe²⁺ binding stabilizes collagen lysyl hydroxylase dimers, although the underlying mechanism remains unclear. Here, we report the crystal structure of an Fe²⁺-binding-deficient mimiviral collagen lysyl hydroxylase, highlighting the conformational changes upon loss of Fe²⁺ binding.

Crystal structure of a recombinant Agaricus bis­porus mushroom mannose-binding protein with a longer C-terminal region

The crystal structure of a variant of recombinant A. bisporus mannose-binding protein with a longer C-terminal region was determined. The flexible C-terminal region may influence the sugar-binding ability.

Crystal structure of ATP-dependent DNA ligase from Rhizobium phage vB_RleM_P10VF

We have determined the structure of the Rhizobium phage vB_RleM_P10VF DNA ligase bound to a nicked DNA duplex to 2.2 Å resolution. The DNA ligase exhibits a canonical DNA ligase-binding mode fully encircling the duplex and has considerable structural homology to T4 DNA ligase and the bacterial ATP-dependent DNA ligase from Prochlorococcus marinus.

Crystal structure of the C1 domain of the surface-layer protein SlpM from Lactobacillus brevis: a module involved in protein self-assembly

The 1.7 Å resolution structure of the C1 domain of the surface-layer protein SlpM from L. brevis is reported. The contact surfaces observed in the crystal lattice potentially contribute to the self-assembly process of SlpM.

Structural analysis of YcdY, a member of the redox-enzyme maturation protein family

YcdY, a putative chaperone of the NarJ subfamily, forms a helix-bundle structure characterized by a dent on the concave side. The dent contains hydrophobic or conserved residues, presumably for the chaperone function of YcdY. Furthermore, we propose that YcdY may function as a chaperone for proteins other than the previously proposed YcdX.