The phosphoenolpyruvate-dependant carbohydrate transport system (PTS) couples uptake of a variety of carbohydrates with phosphorylation in prokaryotes. In this system, a phosphoryl group is sequentially transferred through two general phosphoryl carrier proteins, enzyme I (EI) and HPr, and a carbohydrate-specific permease enzyme II (EII). EII is constituted of two cytoplasmic domains IIA and IIB, and a transmembrane channel IIC domain. The galactitol-specific transporter (IIgat) belongs to the glucitol family and is structurally the least well-known. Nuclear Magnetic Resonance (NMR) spectroscopy was used to solve the three-dimensional structure of IIBGat. IIB Gat is composed of a central four-stranded parallel beta sheet flanked by alpha helices on both sides. NMR titrations and isothermal titration calorimetry (ITC) with IIAGat allowed the identification of the binding interface and preliminary modeling of the structure of the IIB Gat - IIAGat heterodimer. IIAGat was also phosphorylated in-vitro, producing several large chemical shift changes, but no changes to the overall structure.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.98525 |
| Date | January 2005 |
| Creators | Young, Chris, 1981- |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Biochemistry.) |
| Rights | © Chris Young, 2005 |
| Relation | alephsysno: 002328815, proquestno: AAIMR24833, Theses scanned by UMI/ProQuest. |
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