NDLI: Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Brzuszkiewicz, Anna Nowak, Elzbieta Dauter, Zbigniew Dauter, Miroslawa Cieslinski, Hubert Dlugolecka, Anna Kur, Józef
Description	Country affiliation: United States Author Affiliation: Brzuszkiewicz A ( Synchrotron Radiation Research Section, MCL, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA.)
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 A. 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.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
DOI	10.1107/S1744309109030826
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 9
Volume Number	65
Language	English
Publisher	Wiley
Publisher Date	2009-09-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Bacterial Proteins Antagonists & Inhibitors Chemistry Carboxylic Ester Hydrolases Enzyme Inhibitors Pharmacology Organophosphonates Organophosphorus Compounds Pseudoalteromonas Enzymology Amino Acid Sequence Crystallography, X-ray Molecular Sequence Data Palmitoyl-coa Hydrolase Protein Structure, Secondary Sequence Alignment Static Electricity Research Support, N.i.h., Extramural Research Support, N.i.h., Intramural Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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