Professor Edward Neill Baker

Research | Current

Research in our group is concerned with determining the molecular basis of biological processes. We focus on the structure and function of proteins, using X-ray crystallography to determine their 3D structures, and various approaches to relate structure to function (kinetics, binding studies, recombinant DNA methods, as appropriate). Some projects are directed towards the design of new therapeutic drugs.

Research is likely to involve

  • Protein purification and crystallisation
  • X-ray crystallography
  • Computer modelling
  • Bioinformatics

Current projects

  • Structure and function of TB proteins
    We are studying the structure and function of proteins isolated from Mycobacterium tuberculosis, the cause of TB. Some of these proteins are targets for the design of new anti-TB drugs. Others will give new insights into the biology of TB (eg. how the organism persists in the lungs). This project will involve genomic analysis and molecular biology and is carried out as part of an international collaboration.
  • Proteins involved in antibiotic resistance
    Many bacteria are resistant to common antibiotics because they contain enzymes that chemically modify and inactivate them. In this project we are working on the structure and function of some of these enzymes, with the aim of designing new inhibitors to block their activity. (With Dr. C. Smith).
  • Structure of human embryonic haemoglobins
    We are investigating the structure of haemoglobins from the earliest stages of human development in order to understand how oxygen affinity is controlled. This project will involve a mix of crystallography, protein chemistry, spectroscopy and kinetics. (With Dr. T. Brittain).
  • Structure and function of ATP dependent enzymes
    We are analysing how ATP is used in several enzymes of medical importance. Our current focus is on FPGS (folylpolyglutamate synthetase) which controls the storage of folic acid in the body, and is a potential target for anti-cancer drugs. (With Dr. C. Smith).
  • Proteins that assist protein folding
    Many proteins require the assistance of other proteins in order to fold correctly into their biologically-active form. This project involves protein disulfide bond isomerases, which help ensure that correct disulfide bonds are formed. The project is potentially important for biotechnology. (With Dr. P. Metcalf).

Areas of expertise

Structural Biology

Selected publications and creative works (Research Outputs)

  • Evans, G. L., Furkert, D. P., Abermil, N., Kundu, P., de Lange, K. M., Parker, E. J., ... Lott, J. S. (2017). Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups. Data in brief, 15, 1019-1029. 10.1016/j.dib.2017.10.051
    Other University of Auckland co-authors: Daniel Furkert, Shaun Lott
  • Evans, G. L., Furkert, D. P., Abermil, N., Kundu, P., de Lange, K. M., Parker, E. J., ... Shaun Lott, J. (2017). Anthranilate phosphoribosyltransferase: Binding determinants for 5'-phospho-alpha-d-ribosyl-1'-pyrophosphate (PRPP) and the implications for inhibitor design. Biochimica et biophysica acta10.1016/j.bbapap.2017.08.018
    Other University of Auckland co-authors: Daniel Furkert, Shaun Lott
  • Oyugi, M. A., Bashiri, G., Baker, E. N., & Johnson-Winters, K. (2017). Mechanistic insights into F420-dependent glucose-6-phosphate dehydrogenase using isotope effects and substrate inhibition studies. Biochimica et biophysica acta10.1016/j.bbapap.2017.08.001
    Other University of Auckland co-authors: Ghader Bashiri
  • Gerth, M. L., Liu, Y., Jiao, W., Zhang, X.-X., Baker, E. N., Lott, J. S., ... Johnston, J. M. (2017). Crystal structure of a bicupin protein HutD involved in histidine utilization in Pseudomonas. Proteins, 85 (8), 1580-1588. 10.1002/prot.25303
    Other University of Auckland co-authors: Jodie Johnston, Shaun Lott
  • Kwon, H., Young, P. G., Squire, C. J., & Baker, E. N. (2017). Engineering a Lys-Asn isopeptide bond into an immunoglobulin-like protein domain enhances its stability. Scientific Reports, 7, 42753-undefined. 10.1038/srep42753
    Other University of Auckland co-authors: Paul Young, Christopher Squire
  • Brader, M. L., Baker, E. N., Dunn, M. F., Laue, T. M., & Carpenter, J. F. (2017). Using X-Ray Crystallography to Simplify and Accelerate Biologics Drug Development. Journal of pharmaceutical sciences, 106 (2), 477-494. 10.1016/j.xphs.2016.10.017
  • Young, P. G., Yosaatmadja, Y., Harris, P. W. R., Leung, I. K. H., Baker, E. N., & Squire, C. J. (2017). Harnessing ester bond chemistry for protein ligation. Chemical Communications, 53 (9), 1502-1505. 10.1039/c6cc09899a
    Other University of Auckland co-authors: Paul Young, Christopher Squire, Ivanhoe Leung, Paul Harris, Yuliana Yosaatmadja
  • Baker, E. N. (2017). Data archiving and availability in an era of open science. IUCrJ, 4 (1), 1-2. 10.1107/S2052252516020340