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Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.
Publication
- A. Brzuszkiewicz
- E. Nowak
- Z. Dauter
- M. Dauter
- H. Cieśliński
- A. Długołęcka
- J. Kur
- Acta Crystallographica Section F-Structural Biology and Crystallization Communications - Year 2009
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...