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Originally published In Press as doi:10.1074/jbc.M007406200 on September 7, 2000

J. Biol. Chem., Vol. 275, Issue 51, 40211-40217, December 22, 2000
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The Crystal Structure of the Escherichia coli MobA Protein Provides Insight into Molybdopterin Guanine Dinucleotide Biosynthesis*

Michael W. Lake, Carrie A. TempleDagger , K. V. RajagopalanDagger , and Hermann Schindelin§

From the Department of Biochemistry and Center for Structural Biology, State University of New York at Stony Brook, Stony Brook, New York 11794-5215 and the Dagger  Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710

The molybdenum cofactor (Moco) is found in a variety of enzymes present in all phyla and comprises a family of related molecules containing molybdopterin (MPT), a tricyclic pyranopterin with a cis-dithiolene group, as the invariant essential moiety. MPT biosynthesis involves a conserved pathway, but some organisms perform additional reactions that modify MPT. In eubacteria, the cofactor is often present in a dinucleotide form combining MPT and a purine or pyrimidine nucleotide via a pyrophosphate linkage. In Escherichia coli, the MobA protein links a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor and can efficiently reconstitute Rhodobacter sphaeroides apo-DMSOR, an enzyme that requires molybdopterin guanine dinucleotide for activity. In this paper, we present the crystal structure of MobA, a protein containing 194 amino acids. The MobA monomer has an alpha /beta architecture in which the N-terminal half of the molecule adopts a Rossman fold. The structure of MobA has striking similarity to Bacillus subtilis SpsA, a nucleotide-diphospho-sugar transferase involved in sporulation. The cocrystal structure of MobA and GTP reveals that the GTP-binding site is located in the N-terminal half of the molecule. Conserved residues located primarily in three signature sequence motifs form crucial interactions with the bound nucleotide. The binding site for MPT is located adjacent to the GTP-binding site in the C-terminal half of the molecule, which contains another set of conserved residues presumably involved in MPT binding.

* This work was supported by National Institutes of Health (NIH) Grants DK54835 (to H. S.) and GM00091 (to K. V. R.). The National Synchrotron Light Source in Brookhaven is supported by the Department of Energy and NIH, and beam line X26C is supported in part by the State University New York at Stony Brook and its Research Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1FR9 and 1FRW) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

§ To whom correspondence should be addressed. Tel.: 631-632-1022; Fax: 631-632-1555; E-mail: hermann.schindelin@sunysb.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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