Dr Sigurd Wilbanks

Senior Lecturer
SigurdWilbanks2
  • Biochemistry Department
  • School of Biomedical Sciences
  • University of Otago
  • P.O. Box 56
  • 710 Cumberland St
  • Dunedin 9054 , New Zealand
  • Tel.: 64 3 479-7850
  • Fax: 64 3 479-7866
  • Email:sigurd.wilbanks@otago.ac.nz
Wilbanks Laboratory

Background

A.B. cum laude in Classics (Latin) at Harvard University. Thesis: Fortuna in Tacitus’ Annales under Richard Thomas.
Ph.D. in Molecular Biology at University of California, Berkeley  Dissertation: Adaptive Variation in Phycoerythrins under Professor Alexander N. Glazer.
Postdoctoral Scholar at Stanford University School of Medicine with Professor David B. McKay

Roles in the Department and University

Director the Macromolecular X-ray Crystallography Suite
Member of the University of Otago Press Editorial Board
Chief Course Advisor for Undergraduates in Biochemistry
Coordinator of 300 level Biochemistry Curriculum
Convenor of BIOC 222 Proteins and Biotechnology
Convenor of BIOC 351 Advanced Protein Biochemistry

Projects and Collaborations

Hsp70 Molecular Chaperones

We study the structure of Hsp 70 chaperones to better understand how interdomain communication and allosteric effects contribute to the recognition and processing of their protein substrates. We employ X-ray crystallography, small-angle X-ray scattering (in collaboration with Dr Thomas Weiss), Förster resonance energy transfer, and single molecule imaging (in collaboration with Drs Daniil Potapova and Andrea Kwakowsky) to determine structure and kinetic behavior of different Hsp70 faimly members. Members of the lab are skilled in molecular cloning, protein purification, enzymology, spectroscopy and X-ray crystallography.

Improved inteins for peptide engineering

Inteins are self-splicing protein domains, encoded by mobile genetic elements. Their self-splicing activity depends on coordination of several independent reactions. In collaboration with Associate Professor Russell Poulter, and Drs Margi Butler and Monica Gerth of this department, we are identifying the structures which link these steps. In conjunction with theses studies we are engineering split inteins for greater utility in the biological production of cyclized or modified peptides and proteins.

Mechanism of cysteine dioxygenase

Cysteine dioxygenase is a physiologically important enzyme with a chemically fascinating active site, composed of a single iron atom bound to three histidine sidechains.  In collaboration with Dr Guy Jameson of the Otago Chemsitry Department, we are using X-ray crystallography, enzyme kinetics and spectroscopy to identify catalytic intermediates and define a reaction pathway.

Macrophage migratory inhibitory factor

A key element in the human inflammatory response, macrophage migratory inhibitory factor is inhibited by dietary isothiocyanates.  In collaboration with Associate Professor Mark Hampton and Dr Joel Tyndall of the University of Otago, we are using X-ray crystallography to investigate the structural basis for binding of these inhibitors, with the goal of designing improved inhibitors. 

Cytochrome c

Mitochondrial cytochrome c is both a crucial electron carrier in energy metabolism but also a signalling molecule for apoptosis.  In collaboration with Dr. Liz Ledgerwood we are elucidating the effects of the first naturally-occurring mutation ever found in this highly conserved enzyme.  Using techniques ranging from a mouse model to X-ray crystallography we have demostrated the effect of this mutation on the ability of cyotchrome c to be released from mitochondria and activate the caspase signalling cascade.

Psb27

Psb27 stabilizes photosystem II during essential repair of photodamaged subunits.  In collaboration with Professor Julian Eaton-Rye, we are studying the physiological role of Psb27 and the structural basis for Psb27 binding to the photosystem II.

PhD projects available in this laboratory

Awards

  • Matthias Fellner
  • 2014, Student Speaker Award, Oxygen Theme meeting at Christchurch School of Medicine
  • Talk title: "A chromogenic assay of substrate depletion by thiol dioxygenases".
  • Matthias Fellner
  • 2013, QMB Redox Meeting Poster prize, 3rd place
  • Egor Tchesnokov
  • 2012, Canadian Institutes of Health Research post doctoral fellowship
  • Samuel Walsh
  • 2011, Smeaton scholarship

Selected Publications

Matthias Fellner, Eleni Siakkou, Abayomi S Faponle, Egor P. Tchesnokov, Sam P de Visser, Sigurd M Wilbanks, and Guy N L Jameson., Influence of cysteine 164 on active site structure in rat cysteine dioxygenase., J Biol Inorg Chem 2016., Link »

Matthias Fellner, Sekotilani Aloi, Egor P. Tchesnokov, Sigurd M Wilbanks, and Guy N L Jameson., Substrate and pH-Dependent Kinetic Profile of 3-Mercaptopropionate Dioxygenase from Pseudomonas aeruginosa., Biochemistry 2016 vol. 55 (9) pp. 1362-1371., Link »

Egor P. Tchesnokov, Matthias Fellner, Eleni Siakkou, Torsten Kleffmann, Lois W Martin, Sekotilani Aloi, Iain L Lamont, Sigurd M Wilbanks, and Guy N L Jameson., The Cysteine Dioxygenase Homologue from Pseudomonas aeruginosa Is a 3-Mercaptopropionate Dioxygenase., J Biol Chem 2015 vol. 290 (40) pp. 24424-24437, Link »

Emma S Spencer, Edward J Dale, Aimée L Gommans, Malcolm T Rutledge, Christine T Vo, Yoshio Nakatani, Allan B Gamble, Robin A J Smith, Sigurd M Wilbanks, Mark B Hampton, and Joel D A Tyndall., Multiple binding modes of isothiocyanates that inhibit macrophage migration inhibitory factor., Eur J Med Chem 2015 vol. 93C pp. 501-510., Link »

Davies, C. G., Fellner, M., Tchesnokov, E. P., Wilbanks, S. M., & Jameson, G. N. L., The Cys-Tyr Cross-Link of Cysteine Dioxygenase Changes the Optimal pH of the Reaction without a Structural Change., Biochemistry (2014) 53(50), 7961–7968, Link »

Antonia Seidel, Heather Parker, Rufus Turner, Nina Dickerhof, Irada S Khalilova, Sigurd M Wilbanks, Anthony J Kettle, and Guy N L Jameson, Uric Acid and thiocyanate as competing substrates of lactoperoxidase., The Journal of biological chemistry 2014 vol. 289 (32) pp. 21937-21949, Link »

Matthias Fellner, Laura M Doughty, Guy N L Jameson, and Sigurd M Wilbanks, A chromogenic assay of substrate depletion by thiol dioxygenases., Analytical biochemistry 2014, Link »

A Seidel, G Jameson, R Turner, A Kettle, and S Wilbanks, Urate as a Potential Physiological Substrate for Lactoperoxidase, Journal of Biological Inorganic Chemistry 2014 vol. 19 pp. S272-S272,

Tracy M Josephs, Ian M Morison, Catherine L Day, Sigurd M Wilbanks, and Elizabeth C Ledgerwood, Enhancing the peroxidase activity of cytochrome c by mutation of residue 41: implications for the peroxidase mechanism and cytochrome c release., The Biochemical journal 2014 vol. 458 (2) pp. 259-265, Link »

Peter D Mabbitt, Sigurd M Wilbanks, and Julian J Eaton-Rye, Structure and function of the hydrophilic Photosystem II assembly proteins: Psb27, Psb28 and Ycf48., Plant physiology and biochemistry : PPB / Societe francaise de physiologie vegetale , Link »

P Mabbitt, S Wilbanks, and J Eaton-Rye, Duplication and divergence of the Psb27 subunit of Photosystem II in the green algal lineage, New Zealand Journal Of Botany 2014 52:74-83, Link »

Richard J Souness, Torsten Kleffmann, Egor P. Tchesnokov, Sigurd M Wilbanks, Geoffrey B Jameson, and Guy N L Jameson, Mechanistic Implications of Persulfenate and Persulfide Binding in the Active Site of Cysteine Dioxygenase., Biochemistry 2013, 52 (43), pp 7606–7617, Link »

Peter D Mabbitt, Julian J Eaton-Rye, and Sigurd M Wilbanks, Mutational analysis of the stability of Psb27 from Synechocystis sp. PCC 6803: implications for models of Psb27 structure and binding to CP43., European biophysics journal : EBJ 2013, Link »

Anshul Awasthi, Adele G. Woolley, Fabienne J Lecomte, Noelyn Hung, Bruce C Baguley, Sigurd M Wilbanks, Aaron R Jeffs, and Joel D A Tyndall, Variable Expression of GLIPR1 Correlates with Invasive Potential in Melanoma Cells., Frontiers in oncology 2013 vol. 3 p. 225, Link »

M Shankar, S.M. Wilbanks, Y Nakatani, B C Monk, and J.D.A. Tyndall, Catalysis product captured in lumazine synthase from the fungal pathogen Candida glabrata, Acta Crystallographica Section D Biological Crystallography 2013 vol. 69 (8) pp. 1580-1586,

Tracy M Josephs, Matthew D Liptak, Gillian Hughes, Alexandra Lo, Rebecca M Smith, Sigurd M Wilbanks, Kara L Bren, and Elizabeth C Ledgerwood, Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination., Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry , Link »

Joel D A JD Tyndall, Hongqi H Lue, Malcolm T MT Rutledge, Jurgen J Bernhagen, Mark B MB Hampton, and Sigurd M SM Wilbanks, Macrophage migration inhibitory factor covalently complexed with phenethyl isothiocyanate, Acta Crystallographica Section F-Structural Biology And Crystallization Communications 2012 vol. 68 (Pt 9) pp. 999-1002, Link »

Robert D Fagerlund, Poh Ling Ooi, and Sigurd M Wilbanks, Soluble expression and purification of tumor suppressor WT1 and its zinc finger domain., Protein Expression and Purification Volume 85, Issue 2, October 2012, Pages 165–172, Link »

Egor P. Tchesnokov, Sigurd M Wilbanks, and Guy N L Jameson, A Strongly Bound High-Spin Iron(II) Coordinates Cysteine and Homocysteine in Cysteine Dioxygenase, Biochemistry 51, 257–264 (2012)., Link »

Siakkou, E., Rutledge, M. T., Wilbanks, S. M. and Jameson, G. N. L. Correlating cross-link formation with enzymatic activity in cysteine dioxygenase. (2011) Biochim. Biophys. Acta Proteins Proteom. 1814: 2003-2009

Liptak, M. D., Fagerlund, R. D., Ledgerwood, E. C., Wilbanks, S. M., Bren, K. L. The Proapoptotic G41S Mutation to Human Cytochrome c Alters the Heme Electronic Structure and Increases the Electron Self-Exchange Rate. (2011) J. Amer. Chem. Soc. 133:1153-1155.

Siakkou, E., Wilbanks, S. M. and Jameson, G. N. L. Simplified cysteine dioxygenase activity assay allows simultaneous quantitation of both substrate and product. (2010) Anal. Biochem. 405: 127-131. 

Jackson, S. A., Fagerlund, R. D., Wilbanks, S. M., and Eaton-Rye, J. J. Crystal Structure of PsbQ from Synechocystis sp. PCC 6803 at 1.8 A˚: Implications for Binding and Function in Cyanobacterial Photosystem II (2010) Biochemistry 49: 2765–2767.

Mabbitt, P. D., Rautureau, G. J. P., Day, C. L.,Wilbanks, S. M., Eaton-Rye, J. J., and Hinds, M. G. Solution Structure of Psb27 from Cyanobacterial Photosystem II (2009) Biochemistry 48: 8771-8773.

Kleffmann, T., Jongkees, S. A. K., Fairweather, G., Wilbanks, S. M. and Jameson, G. N. L. Mass-spectrometric characterization of two posttranslational modifications of cysteine dioxygenase (2009) J. Biol. Inorg. Chem. 14: 913-921.

Morison, I. M., Cramer Bordé, E. M., Cheesman, E. J., Cheong, P. L., Holyoake, A. J., Fichelson, S., Weeks, R. J., Lo, A., Davies, S. M. K., Wilbanks, S. M., Fagerlund, R. D., Ludgate, M. W., da Silva Tatley, F., Coker, M. S. A., Bockett, N. A., Hughes, G., Pippig, D. A., Smith, M. P., Capron, C. and Ledgerwood, E. C. A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia (2008) Nat. Genet. 40: 387-389. 

E. J. Pearl, A. A. M. Bokor, M. I. Butler, R. T. M. Poulter and S. M. Wilbanks. Preceding hydrophobic and beta-branched amino acids attenuate splicing by the CnePRP8 intein (2007) Biochim. Biophys. Acta Prot. Proteom. 1774, 995-1001.

E. J. Pearl, Joel D. A. Tyndall, R. T. M. Poulter and S. M. Wilbanks. Sequence requirements for splicing by the CnePRP8 intein (2007) FEBS Letters 581, 3000-3004.

F. Schlünzen, D. N. Wilson, P. Tian, J. M. Harms, S. J. McInnes, H. A. S. Hansen, R. Albrecht, J. Buerger. S. M. Wilbanks and P. Fucini. The Binding Mode of the Trigger Factor on the Ribosome: Implications for Protein Folding and SRP Interaction (2005) Structure 13, 1685-1694.

C. R. MacKenzie, S. M. Wilbanks and K. M. McGrath. Superimposed effect of kinetics and echinoderm glycoproteins on heirarchical growth of calcium carbonate (2004) Journal of Materials Chemistry 14, 1238-1244.