A 7.4-A projection structure of outer membrane phospholipase A from Escherichia coli by electron crystallography.
Outer membrane phospholipase A (OMPLA) is one of the few enzymes present in the outer membrane of Escherichia coli. Two-dimensional crystals of OMPLA were grown by reconstitution of purified protein into lipid bilayers via detergent dialysis and were studied by electron crystallography. A 7.4-A projection map reveals OMPLA molecules exhibiting an oval-shaped domain of 30 x 20 A resembling the beta-barrel structure characteristic of porins, which is associated with a 25-A elongated domain of lower density.
Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, Groningen, NL-9747 AG, The Netherlands.
E J
EJ
Boekema
M
M
Stuart
R I
RI
Koning
W
W
Keegstra
A
A
Brisson
H M
HM
Verheij
N
N
Dekker
D001425:Bacterial Outer Membrane Proteins / Q000648:ultrastructure*; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D008051:Lipid Bilayers / Q000378:metabolism; D008854:Microscopy, Electron; D010741:Phospholipases A / Q000648:ultrastructure*; D018272:Porins / Q000737:chemistry; D017433:Protein Structure, Secondary
D001425:Bacterial Outer Membrane Proteins; D008051:Lipid Bilayers; D018272:Porins; D010741:Phospholipases A