1NVJ
Deletion Mutant (Delta 141) of Molybdopterin Synthase
Summary for 1NVJ
| Entry DOI | 10.2210/pdb1nvj/pdb |
| Related | 1FM0 1FMA |
| Descriptor | Molybdopterin converting factor subunit 2, GLYCEROL, FORMIC ACID, ... (5 entities in total) |
| Functional Keywords | deletion mutant, molybdenum cofactor biosynthesis, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 6 |
| Total formula weight | 95909.31 |
| Authors | Rudolph, M.J.,Wuebbens, M.M.,Turque, O.,Rajagopalan, K.V.,Schindelin, H. (deposition date: 2003-02-03, release date: 2003-05-06, Last modification date: 2023-08-16) |
| Primary citation | Rudolph, M.J.,Wuebbens, M.M.,Turque, O.,Rajagopalan, K.V.,Schindelin, H. Structural Studies of Molybdopterin Synthase Provide Insights into its Catalytic Mechanism J.Biol.Chem., 278:14514-14522, 2003 Cited by PubMed Abstract: Molybdenum cofactor biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes, including humans. Genetic deficiencies of enzymes involved in cofactor biosynthesis in humans lead to a severe and usually fatal disease. The molybdenum cofactor contains a tricyclic pyranopterin, termed molybdopterin, that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of molybdopterin is generated by molybdopterin synthase, which consists of a large (MoaE) and small (MoaD) subunit. The crystal structure of molybdopterin synthase revealed a heterotetrameric enzyme in which the C terminus of each MoaD subunit is deeply inserted into a MoaE subunit to form the active site. In the activated form of the enzyme, the MoaD C terminus is present as a thiocarboxylate. The present study identified the position of the thiocarboxylate sulfur by exploiting the anomalous signal originating from the sulfur atom. The structure of molybdopterin synthase in a novel crystal form revealed a binding pocket for the terminal phosphate of molybdopterin, the product of the enzyme, and suggested a binding site for the pterin moiety present in precursor Z and molybdopterin. Finally, the crystal structure of the MoaE homodimer provides insights into the conformational changes accompanying binding of the MoaD subunit. PubMed: 12571227DOI: 10.1074/jbc.M300449200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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