Structural highlights
Function
[MOEB_ECOLI] Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD.[1] [2] [MOAD_ECOLI] Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.[3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leimkuhler S, Rajagopalan KV. A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J Biol Chem. 2001 Jun 22;276(25):22024-31. Epub 2001 Apr 4. PMID:11290749 doi:http://dx.doi.org/10.1074/jbc.M102072200
- ↑ Leimkuhler S, Wuebbens MM, Rajagopalan KV. Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor. J Biol Chem. 2001 Sep 14;276(37):34695-701. Epub 2001 Jul 19. PMID:11463785 doi:http://dx.doi.org/10.1074/jbc.M102787200
- ↑ Schmitz J, Wuebbens MM, Rajagopalan KV, Leimkuhler S. Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold. Biochemistry. 2007 Jan 23;46(3):909-16. PMID:17223713 doi:http://dx.doi.org/10.1021/bi062011w
- ↑ Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature. 2001 Nov 15;414(6861):325-9. PMID:11713534 doi:http://dx.doi.org/10.1038/35104586
