6GBC

The Structure of variant R369A of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdate

Summary for 6GBC

• Entry DOI: 10.2210/pdb6gbc/pdb
• Descriptor: Molybdopterin biosynthesis protein CNX1, ADENOSINE MONOPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: arabidopsis, arabidopsis proteins, coenzymes, metalloproteins, catalytic domain, nucleotide binding, entropic enzyme, adenosine monophosphate, transferase
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 1
• Total formula weight: 49592.83

Authors

Krausze, J. (deposition date: 2018-04-13, release date: 2018-07-18, Last modification date: 2024-01-17)

Primary citation

Krausze, J.,Hercher, T.W.,Zwerschke, D.,Kirk, M.L.,Blankenfeldt, W.,Mendel, R.R.,Kruse, T.
The functional principle of eukaryotic molybdenum insertases.
Biochem. J., 475:1739-1753, 2018

PubMed Abstract: The molybdenum cofactor (Moco) is a redox-active prosthetic group found in the active site of Moco-dependent enzymes, which are vitally important for life. Moco biosynthesis involves several enzymes that catalyze the subsequent conversion of GTP into cyclic pyranopterin monophosphate (cPMP), molybdopterin (MPT), adenylated MPT (MPT-AMP), and finally Moco. While the underlying principles of cPMP, MPT, and MPT-AMP formation are well understood, the molybdenum insertase (Mo-insertase)-catalyzed final Moco maturation step is not. In the present study, we analyzed high-resolution X-ray datasets of the plant Mo-insertase Cnx1E that revealed two molybdate-binding sites within the active site, hence improving the current view on Cnx1E functionality. The presence of molybdate anions in either of these sites is tied to a distinctive backbone conformation, which we suggest to be essential for Mo-insertase molybdate selectivity and insertion efficiency.

PubMed: 29717023
DOI: 10.1042/BCJ20170935

Experimental method

X-RAY DIFFRACTION (1.59 Å)