Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1JW9

Structure of the Native MoeB-MoaD Protein Complex

Summary for 1JW9
Entry DOI10.2210/pdb1jw9/pdb
Related1FMO 1JWA 1JWB
DescriptorMOLYBDOPTERIN BIOSYNTHESIS MOEB PROTEIN, MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1, ZINC ION, ... (5 entities in total)
Functional Keywordsmoeb: modified rossmann fold; (2) cys-x-x-cys zinc-binding motifs; moad: ubiquitin-like fold, ligase
Biological sourceEscherichia coli
More
Total number of polymer chains2
Total formula weight35860.27
Authors
Lake, M.W.,Wuebbens, M.M.,Rajagopalan, K.V.,Schindelin, H. (deposition date: 2001-09-03, release date: 2001-11-21, Last modification date: 2024-02-07)
Primary citationLake, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon