1UUX

Structure of a molybdopterin-bound cnx1g domain links molybdenum and copper metabolism

1UUX の概要

• エントリーDOI: 10.2210/pdb1uux/pdb
• 関連するPDBエントリー: 1EAV 1O8N 1O8O 1O8Q 1UUY
• 分子名称: 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)
• 機能のキーワード: chelatase, molybdenum cofactor biosynthesis
• 由来する生物種: ARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17846.99

構造登録者

Kuper, J.,Llamas, A.,Hecht, H.J.,Mendel, R.R.,Schwarz, G. (登録日: 2004-01-12, 公開日: 2004-08-09, 最終更新日: 2023-12-13)

主引用文献

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

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: 15306815
DOI: 10.1038/NATURE02681

実験手法

X-RAY DIFFRACTION (1.6 Å)