5G2R

Crystal structure of the Mo-insertase domain Cnx1E from Arabidopsis thaliana

5G2R の概要

• エントリーDOI: 10.2210/pdb5g2r/pdb
• 関連するPDBエントリー: 5G2S
• 分子名称: MOLYBDOPTERIN BIOSYNTHESIS PROTEIN CNX1, SULFATE ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: transferase, cnx1, cnx1e, gephyrin, gephe, molybdenum metabolism, moea, mo-insertase, moco, molybdenum cofactor
• 由来する生物種: ARABIDOPSIS THALIANA (THALE CRESS)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49999.86

構造登録者

Krausze, J.,Saha, S.,Probst, C.,Kruse, T.,Heinz, D.W.,Mendel, R.R. (登録日: 2016-04-13, 公開日: 2017-02-15, 最終更新日: 2024-01-10)

主引用文献

Krausze, J.,Probst, C.,Curth, U.,Reichelt, J.,Saha, S.,Schafflik, D.,Heinz, D.W.,Mendel, R.R.,Kruse, T.
Dimerization of the Plant Molybdenum Insertase Cnx1E is Required for Synthesis of the Molybdenum Cofactor.
Biochem.J., 474:163-, 2017

PubMed Abstract: The molybdenum cofactor (Moco) is a redox active prosthetic group, essentially required for numerous enzyme-catalyzed two electron transfer reactions. Moco is synthesized by an evolutionarily old and highly conserved multistep pathway. In the last step of Moco biosynthesis, the molybdenum center is inserted into the final Moco precursor adenylated molybdopterin (MPT-AMP). This unique and yet poorly characterized maturation reaction finally yields physiologically active Moco. In the model plant Arabidopsis, the two domain enzyme, Cnx1, is required for Moco formation. Recently, a genetic screen identified novel Arabidopsis cnx1 mutant plant lines each harboring a single amino acid exchange in the N-terminal Cnx1E domain. Biochemical characterization of the respective recombinant Cnx1E variants revealed two different amino acid exchanges (S197F and G175D) that impair Cnx1E dimerization, thus linking Cnx1E oligomerization to Cnx1 functionality. Analysis of the Cnx1E structure identified Cnx1E active site-bound molybdate and magnesium ions, which allowed to fine-map the Cnx1E MPT-AMP-binding site.

PubMed: 27803248
DOI: 10.1042/BCJ20160846

実験手法

X-RAY DIFFRACTION (2.45 Å)