1JW9

Structure of the Native MoeB-MoaD Protein Complex

1JW9 の概要

• エントリーDOI: 10.2210/pdb1jw9/pdb
• 関連するPDBエントリー: 1FMO 1JWA 1JWB
• 分子名称: MOLYBDOPTERIN BIOSYNTHESIS MOEB PROTEIN, MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1, ZINC ION, ... (5 entities in total)
• 機能のキーワード: moeb: modified rossmann fold; (2) cys-x-x-cys zinc-binding motifs; moad: ubiquitin-like fold, ligase
• 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: 35860.27

構造登録者

Lake, M.W.,Wuebbens, M.M.,Rajagopalan, K.V.,Schindelin, H. (登録日: 2001-09-03, 公開日: 2001-11-21, 最終更新日: 2024-02-07)

主引用文献

Lake, M.W.,Wuebbens, M.M.,Rajagopalan, K.V.,Schindelin, H.
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.
Nature, 414:325-329, 2001

PubMed Abstract: The activation of ubiquitin and related protein modifiers is catalysed by members of the E1 enzyme family that use ATP for the covalent self-attachment of the modifiers to a conserved cysteine. The Escherichia coli proteins MoeB and MoaD are involved in molybdenum cofactor (Moco) biosynthesis, an evolutionarily conserved pathway. The MoeB- and E1-catalysed reactions are mechanistically similar, and despite a lack of sequence similarity, MoaD and ubiquitin display the same fold including a conserved carboxy-terminal Gly-Gly motif. Similar to the E1 enzymes, MoeB activates the C terminus of MoaD to form an acyl-adenylate. Subsequently, a sulphurtransferase converts the MoaD acyl-adenylate to a thiocarboxylate that acts as the sulphur donor during Moco biosynthesis. These findings suggest that ubiquitin and E1 are derived from two ancestral genes closely related to moaD and moeB. Here we present the crystal structures of the MoeB-MoaD complex in its apo, ATP-bound, and MoaD-adenylate forms, and highlight the functional similarities between the MoeB- and E1-substrate complexes. These structures provide a molecular framework for understanding the activation of ubiquitin, Rub, SUMO and the sulphur incorporation step during Moco and thiamine biosynthesis.

PubMed: 11713534
DOI: 10.1038/35104586

実験手法

X-RAY DIFFRACTION (1.7 Å)