TY - JOUR
T1 - Structure of a putative 2′-5′ RNA ligase from Pyrococcus horikoshii
AU - Rehse, Peter H.
AU - Tahirov, Tahir H.
PY - 2005/9
Y1 - 2005/9
N2 - Cyclic phosphodiesterase and 2′-5′ RNA ligase are members of a superfamily of proteins which share structural similarities even though their homology may be very low. A putative 2′-5′ RNA ligase from Pyrococcus horikoshii has been crystallized and its X-ray crystallographic structure determined to 2.4 Å. The protein crystallized in the orthorhombic space group P212121, with unit-cell parameters a = 44.07, b = 45.47, c = 93.17 Å and one protein monomer in the asymmetric unit. The molecular-replacement probe was a 2′-5′ RNA ligase from Thermus thermophilus which shares 30% sequence identity. The P. horikoshii RNA ligase has some structural features that have more in common with a cyclic phosphodiesterase from Arabidopsis thaliana with which it has no significant homology, yet an examination of the electrostatic surface potential clearly defines its relationship to the T. thermophilus RNA ligase. However, the size of the active-site cleft is smaller and less positively charged than that of the T. thermophilus homologue, suggesting that the actual substrate may be smaller than that previously postulated for the latter.
AB - Cyclic phosphodiesterase and 2′-5′ RNA ligase are members of a superfamily of proteins which share structural similarities even though their homology may be very low. A putative 2′-5′ RNA ligase from Pyrococcus horikoshii has been crystallized and its X-ray crystallographic structure determined to 2.4 Å. The protein crystallized in the orthorhombic space group P212121, with unit-cell parameters a = 44.07, b = 45.47, c = 93.17 Å and one protein monomer in the asymmetric unit. The molecular-replacement probe was a 2′-5′ RNA ligase from Thermus thermophilus which shares 30% sequence identity. The P. horikoshii RNA ligase has some structural features that have more in common with a cyclic phosphodiesterase from Arabidopsis thaliana with which it has no significant homology, yet an examination of the electrostatic surface potential clearly defines its relationship to the T. thermophilus RNA ligase. However, the size of the active-site cleft is smaller and less positively charged than that of the T. thermophilus homologue, suggesting that the actual substrate may be smaller than that previously postulated for the latter.
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U2 - 10.1107/S0907444905017841
DO - 10.1107/S0907444905017841
M3 - Article
C2 - 16131753
AN - SCOPUS:32944457550
SN - 0907-4449
VL - 61
SP - 1207
EP - 1212
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 9
ER -