6iv5 | pdb_00006iv5

Crystal structure of arabidopsis N6-mAMP deaminase MAPDA

spinqualitylabelsall models 6iv5, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6iv5 is a 1 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4, ZN Gene: At4g04880, T4B21.20, T4B21_20 (ARATH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Arabidopsis 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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