Structural Insights into the Extracytoplasmic Thiamine-Binding Lipoprotein p37 of Mycoplasma hyorhinis

Katherine H. Sippel, Arthur H. Robbins, Robbie Reutzel, Susan K. Boehlein, Kazunori Namiki, Steve Goodison, Mavis Agbandje-McKenna, Charles J. Rosser, Robert McKenna

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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-A°-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.

Original languageEnglish (US)
Pages (from-to)2585-2592
Number of pages8
JournalJournal of Bacteriology
Issue number8
StatePublished - Apr 2009

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology


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