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Inne
Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.
Autorzy
Rok wydania
2009
Czasopismo
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Numer woluminu
F65
Strony
862-865
DOI
10.1107/S1744309109030826
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
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.
Adres publiczny
http://dx.doi.org/10.1107/S1744309109030826