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J. Biol. Chem., Vol. 279, Issue 53, 55644-55650, December 31, 2004

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Structural Evidence That the 32-Kilodalton Lipoprotein (Tp32) of Treponema pallidum Is an L-Methionine-binding Protein^*

Ranjit K. Deka, Lori Neil, Kayla E. Hagman, Mischa Machius, Diana R. Tomchick, Chad A. Brautigam, and Michael V. Norgard¶

From the Departments of Microbiology and Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390

A structure-to-function approach was undertaken to gain insights into the potential function of the 32-kDa membrane lipoprotein (Tp32) of Treponema pallidum, the syphilis bacterium. The crystal structure of rTp32 (determined at a resolution of 1.85 Å) shows that the organization of rTp32 is similar to other periplasmic ligand-binding proteins (PLBPs), in that it consists of two / domains, linked by two crossovers, with a binding pocket between them. In the pocket, a molecule of L-methionine was detected in the electron density map. Residues from both domains interact with the ligand. One of the crossover regions is comprised of a 3₁₀-helix, a feature not typical in other ligand-binding proteins. Sequence comparison shows strong similarity to other hypothetical methionine-binding proteins. Together, the data support the notion that rTp32 is a component of a periplasmic methionine uptake transporter system in T. pallidum.

Received for publication, August 12, 2004 , and in revised form, October 13, 2004.

The atomic coordinates and structure factors (code 1XS5) 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 by Grant AI-56305 from the NIAID, National Institutes of Health. Use of the Argonne National Laboratory Structural Biology Center beamlines at the Advanced Photon Source was supported by the United State Department of Energy, Office of Energy Research, under contract number W-31-109-ENG-38. 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.

^¶ To whom correspondence should be addressed: Dept. of Microbiology, U.T. Southwestern Medical Center, 6000 Harry Hines Blvd., Dallas, TX 75390. Tel.: 214-648-5900; Fax: 214-648-5905; E-mail: michael.norgard{at}utsouthwestern.edu.

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