Crystallization and preliminary x-ray studies of flavocetin-A, a platelet glycoprotein Ib-binding protein from the habu snake venom.
Flavocetin-A (FL-A) is a platelet glycoprotein Ib-binding protein, a high molecular mass oligomer (149 kDa) of C-type lectin-like subunits alpha and beta isolated from the habu snake venom. Purified FL-A crystallized in the tetragonal space group I4 with unit-cell dimensions a = b = 121.0, c = 63.2 A. The crystals diffract to at least 2.4 A resolution. The structure has been solved by molecular replacement using the crystal structure of factors IX/X-binding protein (PDB code 1ixx) as a search model. The asymmetric unit contains one heterodimer, showing that FL-A is a novel tetradimer (alphabeta)(4) composed of four heterodimers related by a crystallographic fourfold axis.
Fukuda
K
K
Institute of Applied Biochemistry, University of Tsukuba, Tsukuba Science City, Ibaraki 305--8572, Japan.
Mizuno
H
H
Atoda
H
H
Morita
T
T
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry*; D003435:Crotalid Venoms / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D011485:Protein Binding; D011487:Protein Conformation; D030162:Reptilian Proteins; D012984:Software; D017841:Trimeresurus; D014757:Viper Venoms / Q000737:chemistry*
D002352:Carrier Proteins; D003435:Crotalid Venoms; D030162:Reptilian Proteins; D014757:Viper Venoms; C402798:flavocetin A; C070302:factor IX-factor X-binding protein, Crotalinae