6Q32
The structure of the Mo-insertase domain Cnx1E (variant S269DD274S) from Arabidopsis thaliana in complex with Moco-AMP
Summary for 6Q32
| Entry DOI | 10.2210/pdb6q32/pdb |
| Descriptor | Molybdopterin biosynthesis protein CNX1, Moco-AMP, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | molybdenum cofactor, moco biosynthesis, mo insertase, moco-amp, accumulating variant, molybdate binding, hydrolase, biosynthetic protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 51001.31 |
| Authors | Krausze, J. (deposition date: 2018-12-03, release date: 2021-02-17, Last modification date: 2024-01-24) |
| Primary citation | Probst, C.,Yang, J.,Krausze, J.,Hercher, T.W.,Richers, C.P.,Spatzal, T.,Kc, K.,Giles, L.J.,Rees, D.C.,Mendel, R.R.,Kirk, M.L.,Kruse, T. Mechanism of molybdate insertion into pterin-based molybdenum cofactors. Nat.Chem., 13:758-765, 2021 Cited by PubMed Abstract: The molybdenum cofactor (Moco) is found in the active site of numerous important enzymes that are critical to biological processes. The bidentate ligand that chelates molybdenum in Moco is the pyranopterin dithiolene (molybdopterin, MPT). However, neither the mechanism of molybdate insertion into MPT nor the structure of Moco prior to its insertion into pyranopterin molybdenum enzymes is known. Here, we report this final maturation step, where adenylated MPT (MPT-AMP) and molybdate are the substrates. X-ray crystallography of the Arabidopsis thaliana Mo-insertase variant Cnx1E S269D D274S identified adenylated Moco (Moco-AMP) as an unexpected intermediate in this reaction sequence. X-ray absorption spectroscopy revealed the first coordination sphere geometry of Moco trapped in the Cnx1E active site. We have used this structural information to deduce a mechanism for molybdate insertion into MPT-AMP. Given their high degree of structural and sequence similarity, we suggest that this mechanism is employed by all eukaryotic Mo-insertases. PubMed: 34183818DOI: 10.1038/s41557-021-00714-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.39 Å) |
Structure validation
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