1jw9
From Proteopedia
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'''Structure of the Native MoeB-MoaD Protein Complex''' | '''Structure of the Native MoeB-MoaD Protein Complex''' | ||
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[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
[[Category: Wuebbens, M M.]] | [[Category: Wuebbens, M M.]] | ||
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Revision as of 19:00, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 22:00:09 2008
