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.
Authors
- A. Brzuszkiewicz,
- E. Nowak,
- Zbigniew Dauter,
- Mirosława Dauter,
- dr hab. inż. Hubert Cieśliński link open in new tab ,
- Anna Długołęcka link open in new tab ,
- prof. dr hab. Józef Kur link open in new tab
Additional information
- Category
- Publikacja w czasopiśmie
- Type
- artykuł w czasopiśmie wyróżnionym w JCR
- Language
- angielski
- Publication year
- 2009
