5G2R

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

Summary for 5G2R

• Entry DOI: 10.2210/pdb5g2r/pdb
• Related: 5G2S
• Descriptor: MOLYBDOPTERIN BIOSYNTHESIS PROTEIN CNX1, SULFATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: transferase, cnx1, cnx1e, gephyrin, gephe, molybdenum metabolism, moea, mo-insertase, moco, molybdenum cofactor
• Biological source: ARABIDOPSIS THALIANA (THALE CRESS)
• Total number of polymer chains: 1
• Total formula weight: 49999.86

Authors

Krausze, J.,Saha, S.,Probst, C.,Kruse, T.,Heinz, D.W.,Mendel, R.R. (deposition date: 2016-04-13, release date: 2017-02-15, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.45 Å)