3HP4

Crystal structure of psychrotrophic esterase EstA from Pseudoalteromonas sp. 643A inhibited by monoethylphosphonate

3HP4 の概要

• エントリーDOI: 10.2210/pdb3hp4/pdb
• 分子名称: GDSL-esterase (2 entities in total)
• 機能のキーワード: esterase, psychrotrophic, monoethylphosphonate, hydrolase
• 由来する生物種: Pseudoalteromonas sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20803.57

構造登録者

Brzuszkiewicz, A.,Nowak, E.,Dauter, Z.,Dauter, M.,Cieslinski, H.,Kur, J. (登録日: 2009-06-03, 公開日: 2009-06-30, 最終更新日: 2023-09-06)

主引用文献

Brzuszkiewicz, A.,Nowak, E.,Dauter, Z.,Dauter, M.,Cieslinski, H.,Dlugolecka, A.,Kur, J.
Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.
Acta Crystallogr.,Sect.F, 65:862-865, 2009

PubMed 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.

PubMed: 19724118
DOI: 10.1107/S1744309109030826

実験手法

X-RAY DIFFRACTION (1.35 Å)