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J. Biol. Chem., Vol. 279, Issue 30, 31599-31605, July 23, 2004

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NMR Structure of a Type IVb Pilin from Salmonella typhi and Its Assembly into Pilus^*

Xing-Fu Xu, Yih-Wan Tan, Lam Lam, Jim Hackett, Mingjie Zhang, and Yu-Keung Mok¶

From the Department of Biological Sciences, National University of Singapore, Singapore 117543 and the Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong

The structure of the N-terminal-truncated Type IVb structural pilin (t-PilS) from Salmonella typhi was determined by NMR. Although topologically similar to the recently determined x-ray structure of pilin from Vibrio cholerae toxin-coregulated pilus, the only Type IVb pilin with known structure, t-PilS contains many distinct structural features. The protein contains an extra pair of -strands in the N-terminal loop that align with the major -strands to form a continuous 7-stranded antiparallel -sheet. The C-terminal disulfide-bonded region of t-PilS is only half the length of that of toxin-coregulated pilus pilin. A model of S. typhi pilus has been proposed and mutagenesis studies suggested that residues on both the loop and the C-terminal disulfide-bonded region of PilS might be involved in binding specificity of the pilus. This model structure reveals an exposed surface between adjacent subunits of PilS that could be a potential binding site for the cystic fibrosis transmembrane conductance regulator.

Received for publication, April 28, 2004 , and in revised form, May 24, 2004.

^* This work was supported by the A*Star BMRC Young Investigator Award (to Y.-K. M.) and by the Academic Research Fund, National University of Singapore. Some of the NMR spectra used in this work were acquired at the 750-MHz NMR spectrometer in Hong Kong University of Science and Technology. 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.

The atomic coordinates and structure factors (code 1Q5F) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

The NMR chemical shifts (accession code 5879) have been deposited in the BioMagResBank (BMRB), Department of Biochemistry, University of Wisconsin, Madison (www.bmrb.wisc.edu.).

^¶ To whom correspondence should be addressed: Dept. of Biological Sciences, 14 Science Dr. 4, National University of Singapore, Singapore 117543. Tel.: 65-68742967; Fax: 65-67792486; E-mail: dbsmokh{at}nus.edu.sg.

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