Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB–MoaD complex

@article{Lake2001MechanismOU,
  title={Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB–MoaD complex},
  author={Michael W. Lake and Margot M. Wuebbens and Krishnan Rajagopalan and Hermann Schindelin},
  journal={Nature},
  year={2001},
  volume={414},
  pages={325-329}
}
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… 

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IscS Functions as a Primary Sulfur-donating Enzyme by Interacting Specifically with MoeB and MoaD in the Biosynthesis of Molybdopterin in Escherichia coli*

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Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans.

In a defined in vitro system for the generation of MPT from precursor Z, the sulfurated form of MOCS3-RLD was able to provide the sulfur for the thiocarboxylation of M OCS2A, the small MPT synthase subunit in humans.

Crystal Structure of the Human Ubiquitin-activating Enzyme 5 (UBA5) Bound to ATP

Structural features are determined that further the understanding of the UBA5 enzyme reaction mechanism and provide insight into the evolution of ubiquitin activation.

The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like β-grasp domains

BackgroundUbiquitin (Ub)-mediated signaling is one of the hallmarks of all eukaryotes. Prokaryotic homologs of Ub (ThiS and MoaD) and E1 ligases have been studied in relation to sulfur incorporation

E1- and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea

A working model for archaea is proposed in which the E1-like UbaA can activate multiple Ubl SAMPs for protein conjugation as well as for sulfur transfer, and a fundamental insight is provided into the diverse cellular functions of the Ubl system.

A Novel Role for Human Nfs1 in the Cytoplasm

The results suggest that cytosolic Nfs1 has an important role in sulfur transfer for the biosynthesis of Moc, the last step of molybdenum cofactor (Moco) biosynthesis in eukaryotes.

Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8

The structure and mutational analysis of human APPBP1–UBA3, the heterodimeric E1 enzyme for NEDD8, is reported here.

Shared function and moonlighting proteins in molybdenum cofactor biosynthesis

An overview of Moco biosynthesis in bacteria and humans is given and the shared function and moonlighting roles of the participating proteins are highlighted.
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