MRNA capping enzyme: Difference between revisions

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 == Structural highlights ==
-The 3D structure of vaccinia virus Mce shows the regulatory subunit or RNA triphosphatase domain which forms a hydrophilic tunnel. The tunnel is lined with charged residues with one half of the internal surface is lined almost exclusively with basic residues and the other half with acidic residues.  The catalytic subunit or guanylyltransferase contains an active site which binds the GTP via two motifs rich in basic residues<ref>PMID:24607143</ref>.
+The 3D structure of vaccinia virus Mce shows the regulatory subunit or RNA triphosphatase domain which forms a hydrophilic tunnel. The tunnel is lined with charged residues with one half of the internal surface is lined almost exclusively with basic residues and the other half with acidic residues.  The structure contains the catalytic subunit or guanylyltransferase which contains the active site that binds the GTP via two motifs rich in basic residues<ref>PMID:24607143</ref>.
 </StructureSection>