6j4t | pdb_00006j4t
Crystal structure of arabidopsis ADAL complexed with IMP
Structural highlights
FunctionADAL_ARATH Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine (PubMed:29884623, PubMed:30721978, PubMed:31318636). Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A) (PubMed:29884623). Does not possess deaminase activity toward adenosine, AMP, N6-methyladenosine, or N6-mATP in vitro (PubMed:29884623).[1] [2] [3] Publication Abstract from PubMedArabidopsis thaliana aminohydrolase (AtADAL) has been shown to be involved in the metabolism of N(6)-methyl-AMP, a proposed intermediate during m(6)A-modified RNA metabolism, which can be subsequently incorporated into newly synthesized RNA by Pol II. It has been proposed that AtADAL will prevent N(6)-methyl-AMP reuse and catabolize it to inosine monophosphate (IMP). Here, we have solved the crystal structures of AtADAL in the apo form and in complex with GMP and IMP in the presence of Zn(2+). We have identified the substrate-binding pocket of AtADAL and compared it with that for adenosine deaminase (ADA), adenine deaminase (ADE) and AMP deaminase (AMPD) from multiple species. The comparisons reveal that plant ADAL1 may have the potential ability to catalyze different alkyl-group substituted substrates. Structure of Arabidopsis thaliana N(6)-methyl-AMP deaminase ADAL with bound GMP and IMP and implications for N(6)-methyl-AMP recognition and processing.,Wu B, Zhang D, Nie H, Shen S, Li Y, Li S RNA Biol. 2019 Jul 18:1-9. doi: 10.1080/15476286.2019.1642712. PMID:31318636[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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