Crystal Structure of dual specific Trm10 construct from Thermococcus kodakaraensis.

Structural and biochemical analysis of the dual-specificity Trm10 enzyme fromThermococcus kodakaraensisprompts reconsideration of its catalytic mechanism.

This is a c-terminal deletion construct of the protein
tRNA (guanine(9)-/adenine(9)-N1)-methyltransferase

MGSSHHHHHHSSGLVPRGSHMKTLADVFREALKEKGISSIGTLSKRFRKSKNKLQDIAIEIVHGKGAVFRVPEKTAVAWD
LNGNRVDGSYYAYAPLAMREKFEPVLTPEELREKLPDWPYFIIDLYHWDKHTQKEKGKIALQVNQSYGLLRDYFTGSELA
VTWANEEFREMFHGPLDRITTYGGPTSEFLKENGINEVVLLDPWAEEVLSEKDFDVKAFIIGGIVDTGGNKKKTTPKIGE
ELESAGIKVRRRKIVLRGDVVGVPDRINRILGIILKMMVEGKSMDEAVYEMQEPLHARWRLRKELPKRATRYMVEGKVYR
VVEKELFDEYSKWLKIRWEDFVKVLRELDLVALERKRIHHLNKI

bacterial expression vector with T7lac promoter
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

Fonds voor Wetenschappelijk Onderzoek (FWO)

Trm10, Dual specificity enzymes, SPOUT, MTases, RNA BINDING PROTEIN

MKTLADVFREALKEKGISSIGTLSKRFRKSKNKLQDIAIEIVHGKGAVFRVPEKTAVAWDLNGNRVDGSYYAYAPLCMRE
KFEPVLTPEELREKLPDWPYFIIDLYHWDKHTQKEKGKICLQVNQSYGLLRDYFTGSELAVTWANEEFREMFHGPLDRIT
TYGGPTSEFLKENGINEVVLLDPWAEEVLSEKDFDVKAFIIGGIVDTGGNKKKTTPKIGEELESAGIKVRRRKIVLRGDV
VGVPDRINRILGIILKMMVEGKSMDEAVYEMQEPLHARWRLRKELPKRATRYMVEGKVYRVVEKELFDEYSKWLKIRWED
FVKVLRELDLVALERKRIHHLNKI