1UUX
Structure of a molybdopterin-bound cnx1g domain links molybdenum and copper metabolism
Summary for 1UUX
| Entry DOI | 10.2210/pdb1uux/pdb |
| Related | 1EAV 1O8N 1O8O 1O8Q 1UUY |
| Descriptor | MOLYBDOPTERIN BIOSYNTHESIS CNX1, PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER, PROPANOIC ACID, ... (7 entities in total) |
| Functional Keywords | chelatase, molybdenum cofactor biosynthesis |
| Biological source | ARABIDOPSIS THALIANA (MOUSE-EAR CRESS) |
| Total number of polymer chains | 1 |
| Total formula weight | 17846.99 |
| Authors | Kuper, J.,Llamas, A.,Hecht, H.J.,Mendel, R.R.,Schwarz, G. (deposition date: 2004-01-12, release date: 2004-08-09, Last modification date: 2023-12-13) |
| Primary citation | Kuper, J.,Llamas, A.,Hecht, H.J.,Mendel, R.R.,Schwarz, G. Structure of a Molybdopterin-Bound Cnx1G Domain Links Molybdenum and Copper Metabolism Nature, 430:803-, 2004 Cited by PubMed Abstract: The molybdenum cofactor is part of the active site of all molybdenum-dependent enzymes, except nitrogenase. The molybdenum cofactor consists of molybdopterin, a phosphorylated pyranopterin, with an ene-dithiolate coordinating molybdenum. The same pyranopterin-based cofactor is involved in metal coordination of the homologous tungsten-containing enzymes found in archea. The molybdenum cofactor is synthesized by a highly conserved biosynthetic pathway. In plants, the multidomain protein Cnx1 catalyses the insertion of molybdenum into molybdopterin. The Cnx1 G domain (Cnx1G), whose crystal structure has been determined in its apo form, binds molybdopterin with high affinity and participates in the catalysis of molybdenum insertion. Here we present two high-resolution crystal structures of Cnx1G in complex with molybdopterin and with adenylated molybdopterin (molybdopterin-AMP), a mechanistically important intermediate. Molybdopterin-AMP is the reaction product of Cnx1G and is subsequently processed in a magnesium-dependent reaction by the amino-terminal E domain of Cnx1 to yield active molybdenum cofactor. The unexpected identification of copper bound to the molybdopterin dithiolate sulphurs in both structures, coupled with the observed copper inhibition of Cnx1G activity, provides a molecular link between molybdenum and copper metabolism. PubMed: 15306815DOI: 10.1038/NATURE02681 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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