| Autor: |
Han BW; Department of Biochemistry, University of Wisconsin-Madison, WI 53706-1544, USA., Bingman CA, Mahnke DK, Sabina RL, Phillips GN Jr |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2005 Aug 01; Vol. 61 (Pt 8), pp. 740-2. Date of Electronic Publication: 2005 Jul 08. |
| DOI: |
10.1107/S1744309105019792 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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