1jw9
From Proteopedia
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Structure of the Native MoeB-MoaD Protein Complex
Overview
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.
About this Structure
1JW9 is a Protein complex structure of sequences from Escherichia coli with ZN and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex., Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H, Nature. 2001 Nov 15;414(6861):325-9. PMID:11713534
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