Publikace detail

Crystal structure of carbonic anhydrase CaNce103p from the pathogenic yeast Candida albicans

Rok: 2018

Druh publikace: článek v odborném periodiku

Název zdroje: BMC Structural Biology

Název nakladatele: BMC

Místo vydání: Londýn

Strana od-do: "14-1"-"14-11"

Tituly:

Jazyk	Název	Abstrakt	Klíčová slova
cze	Krystalová stuktura karbonické anhydrázy CaNce103p z patogenní kvasinky Candida albicans	Karbonická anhydráza CaNce103p byla připravena rekombinantní expresí v bakteriích Escherichia coli, purifikována a krystlizována. Pomocí rentgenové difrakce byla určena její stuktura, která ukázala, že se jedná o karbonickou anhydrázu typu beta, která je uspořádána jako homotetramer.	karbonická anhydráza; Candida albicans; krystalová struktura; CaNce103p; substrátový tunel
eng	Crystal structure of carbonic anhydrase CaNce103p from the pathogenic yeast Candida albicans	Background: The pathogenic yeast Candida albicans can proliferate in environments with different carbon dioxide concentrations thanks to the carbonic anhydrase CaNce103p, which accelerates spontaneous conversion of carbon dioxide to bicarbonate and vice versa. Without functional CaNce103p, C. albicans cannot survive in atmospheric air. CaNce103p falls into the β-carbonic anhydrase class, along with its ortholog ScNce103p from Saccharomyces cerevisiae. The crystal structure of CaNce103p is of interest because this enzyme is a potential target for surface disinfectants. Results: Recombinant CaNce103p was prepared in E. coli, and its crystal structure was determined at 2.2 Å resolution. CaNce103p forms a homotetramer organized as a dimer of dimers, in which the dimerization and tetramerization surfaces are perpendicular. Although the physiological role of CaNce103p is similar to that of ScNce103p from baker’s yeast, on the structural level it more closely resembles carbonic anhydrase from the saprophytic fungus Sordaria macrospora, which is also tetrameric. Dimerization is mediated by two helices in the N-terminal domain of the subunits. The N-terminus of CaNce103p is flexible, and crystals were obtained only upon truncation of the first 29 amino acids. Analysis of CaNce103p variants truncated by 29, 48 and 61 amino acids showed that residues 30–48 are essential for dimerization. Each subunit contains a zinc atom in the active site and displays features characteristic of type I β-carbonic anhydrases. Zinc is tetrahedrally coordinated by one histidine residue, two cysteine residues and a molecule of β-mercaptoethanol originating from the crystallization buffer. The active sites are accessible via substrate tunnels, which are slightly longer and narrower than those observed in other fungal carbonic anhydrases. Conclusions: CaNce103p is a β-class homotetrameric metalloenzyme composed of two homodimers. Its structure closely resembles those of other β-type carbonic anhydra	Carbonic anhydrase; Candida albicans; Crystal structure; CaNce103p; Substrate tunnel

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