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 Cited by 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: 19724118DOI: 10.1107/S1744309109030826 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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