Structure reveals the activation mechanism of the MC4 receptor to initiate satiation signaling.

Obesity is a global epidemic that causes morbidity and impaired quality of life. The melanocortin receptor 4 (MC4R) is at the crux of appetite, energy homeostasis, and body-weight control in the central nervous system and is a prime target for anti-obesity drugs. Here, we present the cryo-electron microscopy (cryo-EM) structure of the human MC4R-G signaling complex bound to the agonist setmelanotide, a cyclic peptide recently approved for the treatment of obesity.

New homologues of Brassicaceae water-soluble chlorophyll proteins shed light on chlorophyll binding, spectral tuning, and molecular evolution.

Type-II water-soluble chlorophyll (Chl) proteins (WSCPs) of Brassicaceae are promising models for understanding how protein sequence and structure affect Chl binding and spectral tuning in photosynthetic Chl-protein complexes. However, to date, their use has been limited by the small number of known WSCPs, which also limited understanding their physiological roles. To overcome these limitations, we performed a phylogenetic analysis to compile a more comprehensive and complete set of natural type-II WSCP homologues.

Harnessing the Profinity eXact™ System for Expression and Purification of Heterologous Proteins in E. coli.

Highly purified recombinant proteins in large quantities are valuable material for biochemical and structural studies. To achieve this goal, versatile tools were developed to increase the expression of the recombinant proteins and to facilitate the purification process. Fusion tags are commonly used for enhancing expression and solubility and some can be used in the purification process.

Fine Tuning of Chlorophyll Spectra by Protein-Induced Ring Deformation.

The ability to tune the light-absorption properties of chlorophylls by their protein environment is the key to the robustness and high efficiency of photosynthetic light-harvesting proteins. Unfortunately, the intricacy of the natural complexes makes it very difficult to identify and isolate specific protein-pigment interactions that underlie the spectral-tuning mechanisms. Herein we identify and demonstrate the tuning mechanism of chlorophyll spectra in type II water-soluble chlorophyll binding proteins from Brassicaceae (WSCPs).

Calnuc: Emerging roles in calcium signaling and human diseases.

Calnuc is a recently discovered multidomain protein with EF-hand calcium binding sites. Several studies have reported various interacting partners for calnuc and, therefore, also different sites of localization in the cell. It interacts with important molecules such as DNA, G protein, COX, and amyloid precursor protein among others in addition to being involved in stress response and trafficking.

Pseudonocardia antarctica sp. nov. an Actinomycetes from McMurdo Dry Valleys, Antarctica.

Strain DVS 5a1 was isolated from a moraine sample from the McMurdo Dry Valleys region of Antarctica. The strain is aerobic, Gram-positive, with white aerial mycelia and brown substrate mycelia, sporulating, has meso-diaminopimelic acid, arabinose and galactose in the cell wall, MK-8 (H4) as the major menaquinone and a mol% G+C content of DNA of 71% thus confirming to the description of the genus Pseudonocardia. Phylogenetic analysis based on the 16S rRNA gene sequence analysis further confirms that DVS 5al which forms a robust clade with P.

Kocuria polaris sp. nov., an orange-pigmented psychrophilic bacterium isolated from an Antarctic cyanobacterial mat sample.

Strain CMS 76orT, an orange-pigmented bacterium, was isolated from a cyanobacterial mat sample from a pond located in McMurdo Dry Valley, Antarctica. On the basis of chemotaxonomic and phylogenetic properties, strain CMS 76orT was identified as a member of the genus Kocuria. It exhibited a 16S rDNA similarity of 99.