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J. Biol. Chem., Vol. 282, Issue 4, 2596-2605, January 26, 2007

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Structural Characterization of the Active Site of the PduO-Type ATP:Co(I)rrinoid Adenosyltransferase from Lactobacillus reuteri^*

Martin St. Maurice¹², Paola E. Mera¹³, María P. Taranto^¶4, Fernando Sesma^¶4, Jorge C. Escalante-Semerena⁵, and Ivan Rayment⁶

From the Departments of Biochemistry and Bacteriology, University of Wisconsin, Madison, Wisconsin 53706 and the ^¶CERELA-CONICET, Tucumán, Argentina 4000

The three-dimensional crystal structure of the PduO-type corrinoid adenosyltransferase from Lactobacillus reuteri (LrPduO) has been solved to 1.68-Å resolution. The functional assignment of LrPduO as a corrinoid adenosyltransferase was confirmed by in vivo and in vitro evidence. The enzyme has an apparent of 2.2 µM and of 0.13 µM and a k_cat of 0.025 s^-1. Co-crystallization of the enzyme with Mg-ATP resulted in well-defined electron density for an N-terminal loop that had been disordered in other PduO-type enzyme structures. This newly defined N-terminal loop makes up the lower portion of the enzyme active site with the other half being contributed from an adjacent subunit. These results provide the first detailed description of the enzyme active site for a PduO-type adenosyltransferase and identify a unique ATP binding motif at the protein N terminus. The molecular architecture at the active site offers valuable new insight into the role of various residues responsible for the human disease methylmalonic aciduria.

Received for publication, October 10, 2006 , and in revised form, November 10, 2006.

The atomic coordinates and structure factors (code 2NT8) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by Grants AR35186 (to I. R.) and GM40313 (to J. C. E.-S.) from the National Institutes of Health. 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.

¹ These two authors contributed equally to this work.

² Supported in part by a fellowship from the Natural Science and Engineering Research Council of Canada (NSERC).

³ Supported in part by Training Grant T32 GM008505-13 (NIGMS, National Institutes of Health).

⁴ Supported in part by Grants CABBIO 2004 and PICT 15016 from ANPCyT (Argentina).

⁵ To whom correspondence may be addressed. E-mail: escalante{at}bact.wisc.edu. ⁶ To whom correspondence may be addressed: Dept. of Biochemistry, 433 Babcock Dr., Madison, WI 53706. Tel.: 608-262-0437; Fax: 608-262-1319; E-mail: Ivan_Rayment{at}biochem.wisc.edu.

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