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J. Biol. Chem., Vol. 279, Issue 40, 42139-42146, October 1, 2004

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The Crystal Structure of Escherichia coli MoaB Suggests a Probable Role in Molybdenum Cofactor Synthesis^*

Ruslan Sanishvili, Steven Beasley¶, Tania Skarina¶, David Glesne||, Andrzej Joachimiak**, Aled Edwards¶, and Alexei Savchenko¶

From the Biosciences, Structural Biology Center, Midwest Center for Sructural Genomics, Argonne National Laboratory, Argonne, Illinois 60439, the ^¶Clinical Genomics Centre/Proteomics, University Health Network, Toronto, Ontario M5G 1L7, Canada, the ^||Energy Systems Division, Argonne National Laboratory, Argonne, Illinois 60439, and the Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G, Canada

The crystal structure of Escherichia coli MoaB was determined by multiwavelength anomalous diffraction phasing and refined at 1.6-Å resolution. The molecule displayed a modified Rossman fold. MoaB is assembled into a hexamer composed of two trimers. The monomers have high structural similarity with two proteins, MogA and MoeA, from the molybdenum cofactor synthesis pathway in E. coli, as well as with domains of mammalian gephyrin and plant Cnx1, which are also involved in molybdopterin synthesis. Structural comparison between these proteins and the amino acid conservation patterns revealed a putative active site in MoaB. The structural analysis of this site allowed to advance several hypothesis that can be tested in further studies.

Received for publication, January 27, 2004

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

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: General Medicine and Cancer Institute Collaborative Access Team (GM/CA CAT), Argonne National Laboratory.

^** To whom correspondence should be addressed. Tel.: 630-252-3926; Fax: 630-252-6126; E-mail: andrzejj{at}anl.gov.

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