Identification of a Thermo-Regulated Glutamine-Binding Protein from Yersinia pestis

Title: Identification of a Thermo-Regulated Glutamine-Binding Protein from Yersinia pestis

Volume: 15 Issue: 9

Author(s): Monique Cosman, Joseph B. Pesavento, Adam Zemla, Peter T. Beernink, Rod Balhorn and Daniel Barsky

Affiliation:

Keywords: Homology modeling, NMR spectroscopy, Yersinia pestis, glutamine binding protein

Abstract: Here we present modeling and NMR spectroscopic evidence that the function of a Yersinia pestis pMT1 plasmid protein, designated as orf38, is most likely a glutamine binding protein. The modeling was homology-based at a very low level of sequence identity (∼ 16%) and involved structural comparison of multiple templates, as well as template-substrate interaction analyses. Transferred nuclear Overhauser and saturation transfer difference experiments were used to characterize the binding of sugars and amino acids to orf38. The identification and characterization of an unknown protein function using the strategy presented here has applicability to a variety of research areas, including functional genomics and proteomics efforts.

Cite this article as:

Cosman Monique, Pesavento B. Joseph, Zemla Adam, Beernink T. Peter, Balhorn Rod and Barsky Daniel, Identification of a Thermo-Regulated Glutamine-Binding Protein from Yersinia pestis, Protein & Peptide Letters 2008; 15 (9) . https://dx.doi.org/10.2174/092986608785849272