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Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.
Abstract
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.
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- Category:
- Articles
- Type:
- artykuł w czasopiśmie wyróżnionym w JCR
- Published in:
-
Acta Crystallographica Section F-Structural Biology and Crystallization Communications
no. 65,
pages 862 - 865,
ISSN: 1744-3091 - Language:
- English
- Publication year:
- 2009
- Bibliographic description:
- Brzuszkiewicz A., Nowak E., Dauter Z., Dauter M., Cieśliński H., Długołęcka A., Kur J.: Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.// Acta Crystallographica Section F-Structural Biology and Crystallization Communications. -Vol. 65, nr. iss. 9 (2009), s.862-865
- Verified by:
- Gdańsk University of Technology
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