Crystallization and preliminary X-ray crystallographic analysis of adenosine 5'-monophosphate deaminase (AMPD) from Arabidopsis thaliana in complex with coformycin 5'-phosphate. Acta Crystallogr Sect F Struct Biol Cryst Commun 2005 Aug 01;61(Pt 8):740-2
Date
03/03/2006Pubmed ID
16511144Pubmed Central ID
PMC1952363DOI
10.1107/S1744309105019792Scopus ID
2-s2.0-33744954138 (requires institutional sign-in at Scopus site) 2 CitationsAbstract
Adenosine 5'-monophosphate deaminase (AMPD) is a eukaryotic enzyme that converts adenosine 5'-monophosphate (AMP) to inosine 5'-monophosphate (IMP) and ammonia. AMPD from Arabidopsis thaliana (AtAMPD) was cloned into the baculoviral transfer vector p2Bac and co-transfected along with a modified baculoviral genome into Spodoptera frugiperda (Sf9) cells. The resulting recombinant baculovirus were plaque-purified, amplified and used to overexpress recombinant AtAMPD. Crystals of purified AtAMPD have been obtained to which coformycin 5'-phosphate, a transition-state inhibitor, is bound. Crystals belong to space group P6(2)22, with unit-cell parameters a = b = 131.325, c = 208.254 A, alpha = beta = 90, gamma = 120 degrees. Diffraction data were collected to 3.34 A resolution from a crystal in complex with coformycin 5'-phosphate and to 4.05 A resolution from a crystal of a mercury derivative.
Author List
Han BW, Bingman CA, Mahnke DK, Sabina RL, Phillips GN JrAuthor
Donna K. Mahnke Research Scientist I in the Pediatrics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AMP DeaminaseArabidopsis
Arabidopsis Proteins
Coformycin
Crystallization
Crystallography, X-Ray
Data Collection
Macromolecular Substances
Organophosphates
