Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution.
The crystal structure of a calcium binding equine lysozyme has been determined at 2.5 A resolution by means of molecular replacement. The energy minimized equine lysozyme as the starting model, was refined with the molecular dynamics program, X-PLOR, and the R factor of the current model was found to be 24% without any water molecules. The conformation of the calcium binding loop is similar to that of alpha-lactalbumin. The profiles of backbone atomic displacements throughout the lysozyme and alpha-lactalbumin superfamilies are comparable as well as their homologous tertiary structures.
Tsuge
H
H
Life Science Research Laboratory, Japan Tobacco, Inc., Kanagawa.
Ago
H
H
Noma
M
M
Nitta
K
K
Sugai
S
S
Miyano
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002135:Calcium-Binding Proteins / Q000032:analysis*; D002417:Cattle; D003461:Crystallography; D006736:Horses / Q000378:metabolism*; D006801:Humans; D008892:Milk / Q000201:enzymology*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000032:analysis*
D002135:Calcium-Binding Proteins; D009113:Muramidase