• King Abdullah University of Science and Technology (KAUST) Featured PhD Programmes
  • University of Glasgow Featured PhD Programmes
  • University of Leeds Featured PhD Programmes
  • University of Glasgow Featured PhD Programmes
  • University of Warwick Featured PhD Programmes
  • University of Edinburgh Featured PhD Programmes
University of Strathclyde Featured PhD Programmes
Ulster University Featured PhD Programmes
University of Bath Featured PhD Programmes
Ulster University Featured PhD Programmes
Barcelona Institute of Science and Technology Featured PhD Programmes

Funded PhD Opportunity in Membrane Protein Structural Biology - 3-D organization and architecture of the Orco/OrX complex

  • Full or part time
  • Application Deadline
    Applications accepted all year round
  • Funded PhD Project (Students Worldwide)
    Funded PhD Project (Students Worldwide)

About This PhD Project

Project Description

We are offering an opportunity to engage in an exciting PhD project that combines biophysical, biochemical and state-of-the art structural investigation of a unique class of ligand-gated membrane channel receptors from insects. These odorant receptors enable insects to exhibit an unmatched sense of smell that is critical to how mates are attracted, food sources identified and hosts located. Insect odorant receptors are complexes of an ion channel-forming subunit, Orco and one of a family of highly divergent odorant “tuning” receptors, OrX (61 to 341 depending on the insect species). A complex of these two subunits with as-yet unknown stoichiometry (German et al., 2013) is capable of both ionotropic and metabotropic signalling (Carraher et al., 2015). The PhD project will aim to reveal for the first time the 3-D organization and architecture of the Orco/OrX complex and the structural basis for how Orco can couple with so many diverse OrX partners.

You will use our established cell-based and cell-free expression approaches to prepare Orco and OrX homomeric and heteromeric complexes in artificial membrane-like environments (Carraher et al., 2013). These will be subject to a variety of biophysical studies to confirm correct folding and subunit stoichiometry and complex size. 3-D structures of the homomeric (Orco) and heteromeric complexes (Orco/Orx) will be generated by single-particle cryo-EM analysis to reveal individual structures and protein-protein interaction at the highest resolution (Radjainia et al. 2010, 2015). This endeavour will utilize the capabilities of a high-resolution 200kV Transmission Electron Microscope (TEM) equipped with field emission gun enabling high-resolution image acquisition.

This project will suit someone with a demonstrated strong background in protein biochemistry, biophysics or structural biology, who is keen to participate in the structural analysis of membrane proteins. There is funding to support a 3-year PhD stipend. The project will be a collaboration between Assoc Prof Alok Mitra (SBS), Dr Colm Carraher and Dr Andrew Kralicek from Plant & Food Research


Assoc Prof Alok Mitra
School of Biological Sciences
University of Auckland

Phone: +64-9-923 8162
Email:
http://unidirectory.auckland.ac.nz/profile/a-mitra

Dr Colm Carraher
Scientist
Molecular Sensing Team
Plant & Food Research

Phone: +64-9-925-7112
Email:

Dr Andrew Kralicek
Science Team Leader
Molecular Sensing Team
Plant & Food Research

Phone: +64-9-925-7115
Email:

References

Carraher C, Newcomb RD, Kralicek AV (2013) The recombinant expression, detergent solubilisation and purification of insect odorant receptor subunits. Protein Expr. Purif. 90:160-169.

Carraher C, Dalziel J, Jordan M, Christie DL, Newcomb RD, Kralicek AV (2015) Towards an understanding of the structural basis for insect olfaction by odorant receptors. Insect Biochem. Mol. Biol. 66:31-41.

German PF, van der Poel S, Carraher C, Kralicek AV, Newcomb RD (2013) Insights into subunit interactions within the insect olfactory receptor complex using FRET. Insect Biochem Mol Biol. 43: 138-145.

Mazdak Radjainia, Hariprasad Venugopal, Ambroise Desfosses, Amy Phillips, Amy Yewdall, Mark Hampton, Juliet Gerrard, and Alok K. Mitra. (2015). Cryo-EM structure of human peroxiredoxin-3 filament reveals the assembly of a putative chaperone. Structure. Apr 22. pii: S0969-2126(15)00123-9. doi: 10.1016/j.str.2015.03.019.

Radjainia, M., Hyun, J-K., Leysath, C. E., Leppla, S. H. and Mitra, A. K. (2010) An anthrax toxin-neutralizing antibody reconfigures the protective antigen heptamer into a supercomplex. Proc. Natl. Acad. Sci. USA. 107:14070-14074.

Email Now

Insert previous message below for editing? 
You haven’t included a message. Providing a specific message means universities will take your enquiry more seriously and helps them provide the information you need.
Why not add a message here
* required field
Send a copy to me for my own records.

Your enquiry has been emailed successfully



Share this page:

Cookie Policy    X