The multiple nucleotide–divalent cation binding modes of Saccharomyces cerevisiae CK2α indicate a possible co-substrate hydrolysis product (ADP/GDP) release pathway

Four crystal structures of S. cerevisiae CK2α (scCK2α) with different nucleotide co-substrates and coordinated divalent cations indicated that scCK2α possesses dual co-substrate specificity, possible multiple nucleotide–divalent cation binding modes and a possible ADP/GDP-release pathway by means of conformational change of β1/G-loop/β2. The presence of a unique insertion loop in scCK2α enhanced the catalytic efficiency of the enzyme by stabilizing the open conformation of the catalytic site.

Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved α-helix for Act1 binding and IL-17 signaling

Crystal structure of the SEFIR domain from human IL-17 receptor A provides new insights into IL-17 signaling.

Structure of the nisin leader peptidase NisP revealing a C-terminal autocleavage activity

A high resolution crystal structure of the nisin leader peptidase NisP is reported, which revealing a C-terminal autocleavage activity.

Structure of Rot, a global regulator of virulence genes in Staphylococcus aureus

The crystal structure of Rot shows a unique pattern of dimerization that differs from that of other SarA homologues.