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Crystallization and preliminary X‐ray analysis of outer membrane phospholipase A from Escherichia coli
Author(s) -
Blaauw Mieke,
Dekker Niek,
Verheij Hubertus M.,
Kalk Kor H.,
Dijkstra Bauke W.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01002-v
Subject(s) - escherichia coli , crystallization , bacterial outer membrane , phospholipase c , enzyme , membrane , peptide sequence , phospholipase , tris , chemistry , amino acid , trigonal crystal system , biochemistry , crystallography , stereochemistry , crystal structure , organic chemistry , gene
The outer membrane phospholipase A (OMPLA) of Escherichia coli is one of the few integral outer membrane proteins displaying enzymatic activity. It is encoded as a mature protein of 269 amino acids preceded by a signal sequence of 20 amino acids. There is no sequence homology with water‐soluble lipases and phospholipases. Crystals of the mature enzyme were obtained at 22°C from 24–28% (vlv) 2‐methyl‐2,4‐pentanediol in Bis‐Tris buffer, pH 5.9–6.0, with 1 mM calcium chloride and 1.5% (w/v) β‐octylglucoside. They have the symmetry of the trigonal spacegroup P3 1 21 (or P3 2 21) with cell dimensions of ). Native crystals diffract to a resolution of 2.6 Å.