Crystallization of the Zalpha domain of the human editing enzyme ADAR1 complexed with a DNA-RNA chimeric oligonucleotide in the left-handed Z-conformation.
The Zalpha domain of human double-stranded RNA adenosine deaminase (ADAR1) has been crystallized with a hexanucleotide containing alternating deoxyribose and ribose furanose sugars. Solution circular dichroism experiments show that this double-stranded chimera (dCrG)(3) initially adopts the right-handed A-conformation. However, addition of stoichiometric amounts of Zalpha causes a rapid transition to the Z-conformation. Raman spectroscopy of crystals of the Zalpha-(dCrG)(3) complex confirm that the chimeric oligonucleotide is stabilized in the Z-conformation. A complete data set has been obtained at 2.5 A resolution. The Zalpha-(dCrG)(3) crystals belong to the tetragonal I422 space group, with unit-cell parameters a = b = 104.2, c = 117.6 A. Work is under way to solve the structure by molecular replacement.
Brown
Bernard A
BA
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Athanasiadis
Alekos
A
Hanlon
Eugene B
EB
Lowenhaupt
Ky
K
Wilbert
Christina M
CM
Rich
Alexander
A
D000243:Adenosine Deaminase / Q000737:chemistry*; D002942:Circular Dichroism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D011487:Protein Conformation; D012313:RNA / Q000737:chemistry*; D017393:RNA Editing; D016601:RNA-Binding Proteins; D013059:Spectrum Analysis, Raman
D016601:RNA-Binding Proteins; D012313:RNA; D004247:DNA; C567955:ADARB1 protein, human; D000243:Adenosine Deaminase