Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6GB0

The Structure of variant K294A of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP

Summary for 6GB0
Entry DOI10.2210/pdb6gb0/pdb
DescriptorMolybdopterin biosynthesis protein CNX1, ADENOSINE MONOPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordsarabidopsis, arabidopsis proteins, coenzymes, metalloproteins, catalytic domain, nucleotide binding, entropic enzyme, adenosine monophosphate, transferase
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Total number of polymer chains1
Total formula weight50225.49
Authors
Krausze, J. (deposition date: 2018-04-13, release date: 2018-07-18, Last modification date: 2024-01-17)
Primary citationKrausze, 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: 29717023
DOI: 10.1042/BCJ20170935
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.814 Å)
Structure validation

227111

건을2024-11-06부터공개중

PDB statisticsPDBj update infoContact PDBjnumon