Crystallization and preliminary X-ray studies of snake gourd lectin: homology with type II ribosome-inactivating proteins.
The lectin from the seeds of snake gourd (Trichosanthes anguina) has been crystallized in two forms using the hanging-drop method. Both the forms are hexagonal, with the asymmetric unit containing one subunit consisting of two polypeptide chains linked through disulfide bridges. Intensity data from one of the forms were collected at room temperature as well as at low temperature to 3 A resolution. Molecular-replacement studies indicate that the lectin is homologous to type II ribosome-inactivating proteins. Partial refinement confirms this conclusion.
Manoj
N
N
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
Jeyaprakash
A A
AA
Pratap
J V
JV
Komath
S S
SS
Kenoth
R
R
Swamy
M J
MJ
Vijayan
M
M
D003460:Crystallization; D018360:Crystallography, X-Ray; D019662:Cucurbitaceae / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry*; D008958:Models, Molecular; D037121:Plant Lectins; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D054790:Ribosome Inactivating Proteins, Type 2
D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins; D054790:Ribosome Inactivating Proteins, Type 2; C093156:ribosome-inactivating protein 2, maize