Full name: | adenosine deaminase, tRNA specific 2 |
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Synonym: | dJ20N2.1, TAD2 |
GI: | 74750199 |
UniProt: | Q7Z6V5 |
Structures: | | 3DH1 | |
Alpha Fold Predicted Structure: | AF-Q7Z6V5-F1 |
Enzyme type: | deaminase |
Title: | Crystal structure of human tRNA-specific adenosine-34 deaminase subunit ADAT2 |
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Classification: | HYDROLASE |
Technique: | X-Ray Diffraction |
Resolution: | 2.8 |
R value free: | 0.256 |
R value observed: | 0.205 |
R value work: | 0.202 |
Pdb Files | 3DH1.pdb |
Pdbx/mmCIF Files | 3DH1.cif |
MEAKAAPKPAASGACSVSAEETEKWMEEAMHMAKEALENTEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVLDWCRQSGKSPSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNERFGGCGSVLNIASADLPNTGRPFQCIPGYRAEEAVEMLKTFYKQENPNAPKSKVRKKECQKS
Multiple mRNA codons can be decoded by a single tRNA via the post-transcriptional modification of tRNA wobble adenosine. In eukaryotes, adenosine-to-inosine modification is catalyzed by ADAR enzyme family (Savva et al. 2012 ). ADAT is a heterodimeric enzyme belonging to this family that acts on tRNAs. Evolutionary models exploring the sequence homology of ADAT and ADARs suggest these tRNA modifying enzymes be ancestral to ADARs enzymes. ADAT is composed of two subunits named ADAT2 and ADAT3. ADAT2 is the catalytic subunit of the ADAT complex. However, several ADAT3 residues are required for the ADAT complex to be functionally active (Ramos-Morales et al. 2021). Mutations in this enzyme cause different diseases, principally related to neurological disorders. ADAT complex modifies up to eight tRNA transcripts in their 34 anticodon adenosine. (Ramos-Morales et al. 2021)
Enter the variants
Position
Original
Variant
Alpha Fold Pdb Files | AF-Q7Z6V5-F1.pdb |
Alpha Fold Pdbx/mmCIF Files | AF-Q7Z6V5-F1.cif |
DSSP Secondary Structures | Q7Z6V5.dssp |