3HP4

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

Summary for 3HP4

• Entry DOI: 10.2210/pdb3hp4/pdb
• Descriptor: GDSL-esterase (2 entities in total)
• Functional Keywords: esterase, psychrotrophic, monoethylphosphonate, hydrolase
• Biological source: Pseudoalteromonas sp.
• Total number of polymer chains: 1
• Total formula weight: 20803.57

Authors

Brzuszkiewicz, A.,Nowak, E.,Dauter, Z.,Dauter, M.,Cieslinski, H.,Kur, J. (deposition date: 2009-06-03, release date: 2009-06-30, Last modification date: 2023-09-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.35 Å)