1FMA

MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)

1FMA の概要

• エントリーDOI: 10.2210/pdb1fma/pdb
• 関連するPDBエントリー: 1FMO
• 分子名称: MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 1, MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 2, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: isopeptide bond, transferase, molybdenum cofactor biosynthesis
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25874.26

構造登録者

Rudolph, M.J.,Wuebbens, M.M.,Rajagolpalan, K.V.,Schindelin, H. (登録日: 2000-08-16, 公開日: 2001-01-17, 最終更新日: 2024-02-07)

主引用文献

Rudolph, M.J.,Wuebbens, M.M.,Rajagopalan, K.V.,Schindelin, H.
Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation.
Nat.Struct.Biol., 8:42-46, 2001

PubMed Abstract: Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes, including humans. Genetic deficiencies of enzymes involved in Moco biosynthesis in humans lead to a severe and usually fatal disease. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of MPT is generated by MPT synthase, which consists of a large and small subunits. The 1.45 A resolution crystal structure of MPT synthase reveals a heterotetrameric protein in which the C-terminus of each small subunit is inserted into a large subunit to form the active site. In the activated form of the enzyme this C-terminus is present as a thiocarboxylate. In the structure of a covalent complex of MPT synthase, an isopeptide bond is present between the C-terminus of the small subunit and a Lys side chain in the large subunit. The strong structural similarity between the small subunit of MPT synthase and ubiquitin provides evidence for the evolutionary antecedence of the Moco biosynthetic pathway to the ubiquitin dependent protein degradation pathway.

PubMed: 11135669
DOI: 10.1038/83034

実験手法

X-RAY DIFFRACTION (1.58 Å)