6J23
Crystal structure of arabidopsis ADAL complexed with GMP
Summary for 6J23
| Entry DOI | 10.2210/pdb6j23/pdb |
| Descriptor | Adenosine/AMP deaminase family protein, GUANOSINE-5'-MONOPHOSPHATE, ZINC ION, ... (4 entities in total) |
| Functional Keywords | m6a, n6-mamp, arabidopsis, zn, gmp, complex, deaminase, hydrolase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 40431.34 |
| Authors | Wu, B.X.,Zhang, D.,Nie, H.B.,Shen, S.L.,Li, S.S.,Patel, D.J. (deposition date: 2018-12-30, release date: 2019-02-27, Last modification date: 2023-11-22) |
| Primary citation | Wu, B.,Zhang, D.,Nie, H.,Shen, S.,Li, Y.,Li, S. Structure ofArabidopsis thaliana N6-methyl-AMP deaminase ADAL with bound GMP and IMP and implications forN6-methyl-AMP recognition and processing. Rna Biol., 16:1504-1512, 2019 Cited by PubMed Abstract: aminohydrolase (ADAL) has been shown to be involved in the metabolism of N-methyl-AMP, a proposed intermediate during mA-modified RNA metabolism, which can be subsequently incorporated into newly synthesized RNA by Pol II. It has been proposed that ADAL will prevent N-methyl-AMP reuse and catabolize it to inosine monophosphate (IMP). Here, we have solved the crystal structures of ADAL in the apo form and in complex with GMP and IMP in the presence of Zn. We have identified the substrate-binding pocket of ADAL 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. PubMed: 31318636DOI: 10.1080/15476286.2019.1642712 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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