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Molecular Enzymology
London Research Institute -Clare Hall Laboratories- -Cancer Research UK- Charity Registration No. 1089464 -Terms and Conditions- |
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| B) Sequence and conserved motifs |
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During their analysis of the Chlorella virus PBCV-1 genome, Li et al., (Virology 212, 134-150, 1995) found an open reading frame which displayed sequence homology with known capping enzymes. Ho et al., (J. Virology 70, 6658-6664, 1996) expressed this protein and demonstrated that it was a fully active capping enzyme. It is a monofunctional, comparatively small capping enzyme of 330 amino acid residues.
1 MVPPTINTGK NITTERAVLT LNGLQIKLHK VVGESRDDIV AKMKDLAMDD
51 HKFPRLPGPN PVSIERKDFE KLKQNKYVVS EKTDGIRFMM FFTRVFGFKV
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101 CTIIDRAMTV YLLPFKNIPR VLFQGSIFDG ELCVDIVEKK FAFVLFDAVV
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151 VSGVTVSQMD LASRFFAMKR SLKEFKNVPE DPAILRYKEW IPLEHPTIIK
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201 DHLKKANAIY HTDGLIIMSV DEPVIYGRNF NLFKLKPGTH HTIDFIIMSE
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251 DGTIGIFDPN LRKNVPVGKL DGYYNKGSIV ECGFADGTWK YIQGRSDKNQ
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301 ANDRLTYEKT LLNIEENITI DELLDLFKWE
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Amino acid sequence of Chlorella virus capping enzyme. Conserved motifs are shown in bold, and residues that are involved in binding GTP through hydrogen bond or van der Waals' interactions are labelled with a star. Amino acid sequence alignments indicate a series of motifs that are conserved in capping enzymes and in DNA and RNA ligases, suggesting a common fold for this class of nucleotidyltransferases.
These capping enzyme homepages were constructed by Kjell.
A) Capping chemistry |