6GB0
The Structure of variant K294A of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP
Summary for 6GB0
Entry DOI | 10.2210/pdb6gb0/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 | 50225.49 |
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 Cited by 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: 29717023DOI: 10.1042/BCJ20170935 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.814 Å) |
Structure validation
Download full validation report