title: Crystallization of the Zalpha domain of the human editing enzyme ADAR1 complexed with a DNA-RNA chimeric oligonucleotide in the left-handed Z-conformation.
abstract: 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.
authors.affiliation: Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
authors.forename: Bernard A
authors.initials: BA
authors.lastname: Brown
authors.forename: Alekos
authors.initials: A
authors.lastname: Athanasiadis
authors.forename: Eugene B
authors.initials: EB
authors.lastname: Hanlon
authors.forename: Ky
authors.initials: K
authors.lastname: Lowenhaupt
authors.forename: Christina M
authors.initials: CM
authors.lastname: Wilbert
authors.forename: Alexander
authors.initials: A
authors.lastname: Rich
mesh_terms: 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
chemical_list: D016601:RNA-Binding Proteins; D012313:RNA; D004247:DNA; C567955:ADARB1 protein, human; D000243:Adenosine Deaminase