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Literature summary for 2.7.7.31 extracted from

  • Gouge, J.; Rosario, S.; Romain, F.; Beguin, P.; Delarue, M.
    Structures of intermediates along the catalytic cycle of terminal deoxynucleotidyltransferase: dynamical aspects of the two-metal ion mechanism (2013), J. Mol. Biol., 425, 4334-4352.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
high-resolution X-ray structures that mimic the pre-catalytic state, the post-catalytic state and a competent state that can be transformed into the two other ones. Zn2+ (or Co2+) in Metal A site changes coordination from octahedral to tetrahedral after the chemical step, which explains the known higher affinity of Tdt for the primer strand when these ions are present, and metal A has to leave to allow the translocation of the primer strand and to clear the active site. Except for Zn2+, the sugar puckering of the primer strand 3' terminus changes from C2'-endo to C3'-endo during catalysis. Metal A is the last component that binds to the active site to complete its productive assembly Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ effect of Mn2+, Co2+ and Zn2+, analysis in X-ray structures that mimic the pre-catalytic state, the post-catalytic state and a competent state Mus musculus
Mn2+ effect of Mn2+, Co2+ and Zn2+, analysis in X-ray structures that mimic the pre-catalytic state, the post-catalytic state and a competent state Mus musculus
Zn2+ effect of Mn2+, Co2+ and Zn2+, analysis in X-ray structures that mimic the pre-catalytic state, the post-catalytic state and a competent state Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus P09838
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-

Synonyms

Synonyms Comment Organism
DNTT
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Mus musculus