1uux

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spinqualitylabelsall models 1uux, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF A MOLYBDOPTERIN-BOUND CNX1G DOMAIN LINKS MOLYBDENUM AND COPPER METABOLISM

Overview

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.

About this Structure

1UUX is a Single protein structure of sequence from Arabidopsis thaliana with CU1, MTE, PPI, IMD and FMT as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism., Kuper J, Llamas A, Hecht HJ, Mendel RR, Schwarz G, Nature. 2004 Aug 12;430(7001):803-6. PMID:15306815

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