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Title: 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 bacterium Pseudoalteromonas sp. 643A was determined in a covalently inhibited form at a resolution of 1.35 {angstrom}. The enzyme has a typical SGNH hydrolase structure consisting of a single domain containing a five-stranded {beta}-sheet, with three helices at the convex side and two helices at the concave side of the sheet, and is ornamented with a couple of very short helices at the domain edges. The active site is located in a groove and contains the classic catalytic triad of Ser, His and Asp. In the structure of the crystal soaked in diethyl p-nitrophenyl phosphate (DNP), the catalytic serine is covalently connected to a phosphonate moiety that clearly has only one ethyl group. This is the only example in the Protein Data Bank of a DNP-inhibited enzyme with covalently bound monoethylphosphate.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1006193
Resource Type:
Journal Article
Journal Name:
Acta Crystallogr. F
Additional Journal Information:
Journal Volume: 65; Journal Issue: (9) ; 09, 2009; Journal ID: ISSN 1744-3091
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; CRYSTAL STRUCTURE; ENZYMES; ESTERASES; HYDROLASES; PHOSPHATES; PHOSPHONATES; PROTEINS; RESOLUTION; SERINE

Citation Formats

Brzuszkiewicz, Anna, Nowak, Elzbieta, Dauter, Zbigniew, Dauter, Miroslawa, Cieslinski, Hubert, Dlugolecka, Anna, Kur, Józef, NIH), and Gdansk). Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate. United States: N. p., 2010. Web. doi:10.1107/S1744309109030826.
Brzuszkiewicz, Anna, Nowak, Elzbieta, Dauter, Zbigniew, Dauter, Miroslawa, Cieslinski, Hubert, Dlugolecka, Anna, Kur, Józef, NIH), & Gdansk). Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate. United States. https://doi.org/10.1107/S1744309109030826
Brzuszkiewicz, Anna, Nowak, Elzbieta, Dauter, Zbigniew, Dauter, Miroslawa, Cieslinski, Hubert, Dlugolecka, Anna, Kur, Józef, NIH), and Gdansk). 2010. "Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate". United States. https://doi.org/10.1107/S1744309109030826.
@article{osti_1006193,
title = {Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate},
author = {Brzuszkiewicz, Anna and Nowak, Elzbieta and Dauter, Zbigniew and Dauter, Miroslawa and Cieslinski, Hubert and Dlugolecka, Anna and Kur, Józef and NIH) and Gdansk)},
abstractNote = {The crystal structure of the esterase EstA from the cold-adapted bacterium Pseudoalteromonas sp. 643A was determined in a covalently inhibited form at a resolution of 1.35 {angstrom}. The enzyme has a typical SGNH hydrolase structure consisting of a single domain containing a five-stranded {beta}-sheet, with three helices at the convex side and two helices at the concave side of the sheet, and is ornamented with a couple of very short helices at the domain edges. The active site is located in a groove and contains the classic catalytic triad of Ser, His and Asp. In the structure of the crystal soaked in diethyl p-nitrophenyl phosphate (DNP), the catalytic serine is covalently connected to a phosphonate moiety that clearly has only one ethyl group. This is the only example in the Protein Data Bank of a DNP-inhibited enzyme with covalently bound monoethylphosphate.},
doi = {10.1107/S1744309109030826},
url = {https://www.osti.gov/biblio/1006193}, journal = {Acta Crystallogr. F},
issn = {1744-3091},
number = (9) ; 09, 2009,
volume = 65,
place = {United States},
year = {Thu Oct 28 00:00:00 EDT 2010},
month = {Thu Oct 28 00:00:00 EDT 2010}
}