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J. Biol. Chem., Vol. 282, Issue 42, 31076-31084, October 19, 2007

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The Structure of the Haemophilus influenzae HMW1 Pro-piece Reveals a Structural Domain Essential for Bacterial Two-partner Secretion^*

Hye-Jeong Yeo¹, Takeshi Yokoyama, Katarzyna Walkiewicz, Youngchang Kim, Susan Grass^¶, and Joseph W. St. Geme, III^¶

From the Department of Biology and Biochemistry, University of Houston, Houston, Texas 77204, the Structural Biology Center, Argonne National Laboratory, Argonne, Illinois 60439, and the ^¶Departments of Pediatrics and Molecular Genetics & Microbiology, Duke University, Medical Center, Durham, North Carolina 27710

In pathogenic Gram-negative bacteria, many virulence factors are secreted via the two-partner secretion pathway, which consists of an exoprotein called TpsA and a cognate outer membrane translocator called TpsB. The HMW1 and HMW2 adhesins are major virulence factors in nontypeable Haemophilus influenzae and are prototype two-partner secretion pathway exoproteins. A key step in the delivery of HMW1 and HMW2 to the bacterial surface involves targeting to the HMW1B and HMW2B outer membrane translocators by an N-terminal region called the secretion domain. Here we present the crystal structure at 1.92Å of the HMW1 pro-piece (HMW1-PP), a region that contains the HMW1 secretion domain and is cleaved and released during HMW1 secretion. Structural analysis of HMW1-PP revealed a right-handed -helix fold containing 12 complete parallel coils and one large extra-helical domain. Comparison of HMW1-PP and the Bordetella pertussis FHA secretion domain (Fha30) reveals limited amino acid homology but shared structural features, suggesting that diverse TpsA proteins have a common structural domain required for targeting to cognate TpsB proteins. Further comparison of HMW1-PP and Fha30 structures may provide insights into the keen specificity of TpsA-TpsB interactions.

Received for publication, July 13, 2007

The atomic coordinates and structure factors (code 2ODL) 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 funds from the Department of Biology and Biochemistry at the University of Houston, Robert. W. Welch Foundation Grant E-1616, National Institutes of Health Grant AI068943 (to H. J. Y.), and National Institutes of Health Grant DC02873 (to J. W. S.). 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 To whom correspondence should be addressed: Dept. of Biology and Biochemistry, University of Houston, Houston, TX 77204. Tel.: 713-743-8377; Fax: 713-743-8351; E-mail: hyeo{at}uh.edu.

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				G. Duret, M. Szymanski, K.-J. Choi, H.-J. Yeo, and A. H. Delcour The TpsB Translocator HMW1B of Haemophilus influenzae Forms a Large Conductance Channel J. Biol. Chem., June 6, 2008; 283(23): 15771 - 15778. [Abstract] [Full Text] [PDF]