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Journal of Bacteriology, April 2009, p. 2585-2592, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.01680-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Structural Insights into the Extracytoplasmic Thiamine-Binding Lipoprotein p37 of Mycoplasma hyorhinis{triangledown} ,{ddagger}

Katherine H. Sippel,1 Arthur H. Robbins,1 Robbie Reutzel,1,{dagger} Susan K. Boehlein,2 Kazunori Namiki,3 Steve Goodison,4 Mavis Agbandje-McKenna,1 Charles J. Rosser,3 and Robert McKenna1*

Department of Biochemistry and Molecular Biology,1 Program in Plant Molecular and Cellular Biology and Horticultural Sciences,2 Department of Urology, University of Florida, Gainesville, Florida 32610,3 Department of Surgery Jacksonville, Shands Health Science Center, Jacksonville, Florida 322094

Received 1 December 2008/ Accepted 9 February 2009

The Mycoplasma hyorhinis protein p37 has been implicated in tumorigenic transformation for more than 20 years. Though there are many speculations as to its function, based solely on sequence homology, the issue has remained unresolved. Presented here is the 1.6-Å-resolution refined crystal structure of M. hyorhinis p37, renamed the extracytoplasmic thiamine-binding lipoprotein (Cypl). The structure shows thiamine pyrophosphate (TPP) and two calcium ions are bound to Cypl and give the first insights into possible functions of the Cypl-like family of proteins. Sequence alignments of Cypl-like proteins between several different species of mycoplasma show that the thiamine-binding site is likely conserved and structural alignments reveal the similarity of Cypl to various binding proteins. While the experimentally determined function of Cypl remains unknown, the structure shows that the protein is a TPP-binding protein, opening up many avenues for future mechanistic studies and making Cypl a possible target for combating mycoplasma infections and tumorigenic transformation.

* Corresponding author. Mailing address: 100 Newell Dr. LG-171, Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610. Phone: (352) 392-5696. Fax: (352) 392-3422. E-mail: rmckenna{at}ufl.edu

{triangledown} Published ahead of print on 20 February 2009.

{ddagger} Supplemental material for this article may be found at http://jb.asm.org/.

{dagger} Present address: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454.

Journal of Bacteriology, April 2009, p. 2585-2592, Vol. 191, No. 8
0021-9193/09/$08.00+0     doi:10.1128/JB.01680-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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