Structural insights into the octamerization of glycerol dehydrogenase.

Glycerol dehydrogenase (GDH) catalyzes glycerol oxidation to dihydroxyacetone in a NAD+-dependent manner. As an initiator of the oxidative pathway of glycerol metabolism, a variety of functional and structural studies of GDH have been conducted previously. Structural studies revealed intriguing features of GDH, like the flexible β-hairpin and its significance.

Structural and functional insights into the flexible β-hairpin of glycerol dehydrogenase.

During glycerol metabolism, the initial step of glycerol oxidation is catalysed by glycerol dehydrogenase (GDH), which converts glycerol to dihydroxyacetone in a NAD -dependent manner via an ordered Bi-Bi kinetic mechanism. Structural studies conducted with GDH from various species have mainly elucidated structural details of the active site and ligand binding. However, the structure of the full GDH complex with both cofactor and substrate bound is not determined, and thus, the structural basis of the kinetic mechanism of GDH remains unclear.

Structural and biochemical insights into Zn-bound EF-hand proteins, EFhd1 and EFhd2.

EF-hand proteins, which contain a Ca-binding EF-hand motif, are involved in regulating diverse cellular functions. Ca binding induces conformational changes that modulate the activities of EF-hand proteins. Moreover, these proteins occasionally modify their activities by coordinating metals other than Ca, including Mg, Pb and Zn, within their EF-hands.

Structural and Biochemical Characterization of EFhd1/Swiprosin-2, an Actin-Binding Protein in Mitochondria.

Ca regulates several cellular functions, including signaling events, energy production, and cell survival. These cellular processes are mediated by Ca-binding proteins, such as EF-hand superfamily proteins. Among the EF-hand superfamily proteins, allograft inflammatory factor-1 (AIF-1) and swiprosin-1/EF-hand domain-containing protein 2 (EFhd2) are cytosolic actin-binding proteins.

Structure of the MICU1-MICU2 heterodimer provides insights into the gatekeeping threshold shift.

Mitochondrial calcium uptake proteins 1 and 2 (MICU1 and MICU2) mediate mitochondrial Ca influx via the mitochondrial calcium uniporter (MCU). Its molecular action for Ca uptake is tightly controlled by the MICU1-MICU2 heterodimer, which comprises Ca sensing proteins which act as gatekeepers at low [Ca] or facilitators at high [Ca]. However, the mechanism underlying the regulation of the Ca gatekeeping threshold for mitochondrial Ca uptake through the MCU by the MICU1-MICU2 heterodimer remains unclear.