6IV5

Crystal structure of arabidopsis N6-mAMP deaminase MAPDA

6IV5 の概要

• エントリーDOI: 10.2210/pdb6iv5/pdb
• 分子名称: Adenosine/AMP deaminase family protein, PHOSPHATE ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: m6a, n6-mamp, arabidopsis, zn, hydrolase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40164.08

構造登録者

Wu, B.X.,Zhang, D.,Nie, H.B.,Shen, S.L.,Li, S.S.,Patel, D.J. (登録日: 2018-12-02, 公開日: 2019-02-27, 最終更新日: 2023-11-22)

主引用文献

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

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: 31318636
DOI: 10.1080/15476286.2019.1642712

実験手法

X-RAY DIFFRACTION (1.749 Å)