AMP-activated protein kinase (AMPK) is a master metabolic regulator for controlling cellular energy homeostasis. Its homolog in yeast, SNF1, is activated in response to glucose depletion and other stresses. The catalytic (alpha) subunit of AMPK/SNF1 in yeast (Snf1) contains a protein Ser/Thr kinase domain (KD), an auto-inhibitory domain (AID) and a region that mediates interactions with the two...

Despite the involvement in diverse physiological process and pleiotropic expression profile, the molecular functions of Nur77 are not likely to be fully elucidated. From the effort to find a novel function of Nur77, we detected molecular interaction between Nur77 and PKC. Details of interaction revealed that C-terminal ligand binding domain (LBD) of Nur77 specifically interacted with highly con...

Shikimate dehydrogenase catalyzes the NADPH-dependent reversible reduction of 3-dehydroshikimate to shikimate. We report the first X-ray structure of shikimate dehydrogenase from Haemophilus influenzae to 2.4-A resolution and its complex with NADPH to 1.95-A resolution. The molecule contains two domains, a catalytic domain with a novel open twisted alpha/beta motif and an NADPH binding domain w...

tyrosinase (ec: 1.14.18.1) is a copper - containing enzyme which is distributed in all domains of life such as prokaryote, eukaryote, mammals, invertebrates and plants. tyrosinase catalyzes the oxidation of monophenols to diphenols and diphenols to o-quinones . the tyrosinase crystallographic data shows two histidine -rich regions named cua and cub. a loop containing residues m374, s375 and v37...

The methionine salvage pathway is ubiquitous in all organisms, but metabolic variations exist between bacteria and mammals. 5-Methylthioribose (MTR) kinase is a key enzyme in methionine salvage in bacteria and the absence of a mammalian homolog suggests that it is a good target for the design of novel antibiotics. The structures of the apo-form of Bacillus subtilis MTR kinase, as well as its AD...

Background: The ivermectin-binding site on the glutamate-gated chloride channel was recently resolved by crystallography. Results: Ivermectin binds in a similar orientation to the structurally-related glycine receptor although two H-bonds apparent in the crystal structure proved unimportant for binding to glycine receptors. Conclusion: Ivermectin binding mechanisms vary among Cys-loop receptors...