1NVI

Orthorhombic Crystal Form of Molybdopterin Synthase

Summary for 1NVI

• Entry DOI: 10.2210/pdb1nvi/pdb
• Related: 1FM0 1FMA
• Descriptor: Molybdopterin converting factor subunit 1, Molybdopterin converting factor subunit 2, SULFATE ION, ... (5 entities in total)
• Functional Keywords: protein-protein complex, molybdenum cofactor biosynthesis, transferase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 26226.25

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

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: 12571227
DOI: 10.1074/jbc.M300449200

Experimental method

X-RAY DIFFRACTION (1.9 Å)