Repozytorium publikacji - Politechnika Gdańska

The crystal structure of the esterase EstA from the cold-adapted bacteriumPseudoalteromonas sp. 643A was determined in a covalently inhibited form at aresolution of 1.35 A˚. The enzyme has a typical SGNH hydrolase structureconsisting of a single domain containing a five-stranded beta-sheet, with threehelices at the convex side and two helices at the concave side of the sheet, and isornamented with a couple of very short helices at the domain edges. The activesite is located in a groove and contains the classic catalytic triad of Ser, His andAsp. In the structure of the crystal soaked in diethyl p-nitrophenyl phosphate(DNP), the catalytic serine is covalently connected to a phosphonate moiety thatclearly has only one ethyl group. This is the only example in the Protein DataBank of a DNP-inhibited enzyme with covalently bound monoethylphosphate.

Autorzy

• A. Brzuszkiewicz,
• E. Nowak,
• Zbigniew Dauter,
• Mirosława Dauter,
• dr hab. inż. Hubert Cieśliński link otwiera się w nowej karcie ,
• Anna Długołęcka link otwiera się w nowej karcie ,
• prof. dr hab. Józef Kur link otwiera się w nowej karcie