Structure and mechanism of Zn^(2+)- transporting P-type ATPases

Zinc is an essential micronutrient for all living organisms. It is required for signalling and proper functioning of a range of proteins involved in, for example, DNA binding and enzymatic catalysis. In prokaryotes and photosynthetic eukaryotes, Zn2+-transporting P-type ATPases of class IB (ZntA) are crucial for cellular redistribution and detoxification of Zn2+ and related elements. Here we present crystal structures representing the phosphoenzyme ground state (E2P) and a dephosphorylation intermediate (E2·P_i) of ZntA from Shigella sonnei, determined at 3.2 Å and 2.7 Å resolution, respectively. The structures reveal a similar fold to Cu^+-ATPases, with an amphipathic helix at the membrane interface. A conserved electronegative funnel connects this region to the intramembranous high-affinity ion-binding site and may promote specific uptake of cellular Zn^(2+) ions by the transporter. The E2P structure displays a wide extracellular release pathway reaching the invariant residues at the high-affinity site, including C392, C394 and D714. The pathway closes in the E2·P_i state, in which D714 interacts with the conserved residue K693, which possibly stimulates Zn^(2+) release as a built-in counter ion, as has been proposed for H^+-ATPases. Indeed, transport studies in liposomes provide experimental support for ZntA activity without counter transport. These findings suggest a mechanistic link between P_(IB)-type Zn^(2+)-ATPases and P_(III)-type H^+-ATPases and at the same time show structural features of the extracellular release pathway that resemble P_(II)-type ATPases such as the sarcoplasmic/endoplasmic reticulum Ca^(2+)-ATPase (SERCA) and Na^+, K^+-ATPase. These findings considerably increase our understanding of zinc transport in cells and represent new possibilities for biotechnology and biomedicine

Study of the competitiveness of industrial parks using conjoint analysis

In an environment of high competition, globalization, war and certain restrictions of the World Trade Organization, Ukraine is forced to look for new ways to revive its economy. Today, one of the tools for the future development of Ukraine’s economy is the creation, development and operation of industrial parks. The article analyzes the market of industrial parks in Ukraine: current state and development prospects. Using the PESTEL analysis, the author studies the factors influencing the strength of competition in this area. The analysis of scientific sources and the results of the authors’ research suggests that the level of competitiveness of industrial parks in Ukraine depends on the rental price of office and production space, the cost of labor in the region, the level of infrastructure development, the developer’s image and the distance to the border with the EU countries. Conjoint analysis is a popular and reliable statistical method for studying the preferences of future consumers of a product or service. With this tool’s help, the article deter-mines the importance of factors that affect the competitiveness of industrial parks in Ukraine. It should be noted that this method also makes it possible to assess the level of competitiveness at given values of each factor, which will allow concentrating the efforts and resources of the en-terprise (industrial park) on increasing the level of the most important ones

Вплив нічного освітлення на анатомічні і фізіологічні властивості листків липи, гіркокаштану і платану у садово-паркових і вуличних насадженнях Києва

The effect of nighttime lighting on the anatomical and morphological structure and the content of photosynthetic pigments in the leaves of Tilia cordata, Aesculus hippocastanum, and Platanus acerifolia was estimated on the example of garden-park and street plantings of Kyiv. At the experimental sites, the level of illumination and the soil surface temperature during the day and night periods were examined. The anatomical and morphological structure of the leaves was studied using transmission electron microscopy. The content of photosynthetic pigments (chlorophylls and carotenoids) in tree leaves was determined spectrophotometrically.The analysis of variance revealed that nighttime lighting significantly affected the anatomical structure and the content of photosynthetic pigments in the leaves of T. cordata and P. acerifolia. In A. hippocastanum, only parameters of stomata and palisade parenchyma showed a significant reaction to this stress factor.Досліджено вплив штучного нічного освітлення на анатомо-морфологічну структуру та вміст фотосинтетичних пігментів в листках насаджень Tilia cordata, Aesculus hippocastanum і Platanus acerifolia на прикладі садово-паркових і вуличних насаджень Києва. На дослідних ділянках реєстрували рівень освітленості, температуру на поверхні ґрунту в денний та нічний періоди. Анатомо-морфологічну структуру листків досліджували за допомогою трансмісійного електронного мікроскопу. Вміст фотосинтетичних пігментів (хлорофілів і каротиноїдів) у листках дерев визначали спектрофотометрично.Результати дисперсійного аналізу показали, що нічне освітлення суттєво впливає на анатомо-морфологічну структуру, а також вміст фотосинтетичних пігментів у листках T. cordata і P. acerifolia. Водночас, в A. hippocastanum лише морфологічні показники продихів і палісадної паренхіми виявили істотну залежність від цього стресового фактору

Copper-transporting P-type ATPases use a unique ion-release pathway

Heavy metals in cells are typically regulated by PIB-type ATPases. The first structure of the class, a Cu(+)-ATPase from Legionella pneumophila (LpCopA), outlined a copper transport pathway across the membrane, which was inferred to be occluded. Here we show by molecular dynamics simulations that extracellular water solvated the transmembrane (TM) domain, results indicative of a Cu(+)-release pathway. Furthermore, a new LpCopA crystal structure determined at 2.8-Å resolution, trapped in the preceding E2P state, delineated the same passage, and site-directed-mutagenesis activity assays support a functional role for the conduit. The structural similarities between the TM domains of the two conformations suggest that Cu(+)-ATPases couple dephosphorylation and ion extrusion differently than do the well-characterized PII-type ATPases. The ion pathway explains why certain Menkes' and Wilson's disease mutations impair protein function and points to a site for inhibitors targeting pathogens