Tews, Ivo - University of Southampton - Discipline of Biological Sciences

个人简介

Career history 2010-2014: Lecturer in Structural Biology. University of Southampton, UK. Postdoctural Research Fellow. Heidelberg University, Germany. Postdoctural Research Fellow. NIMR Mill Hill, London, UK. Academic qualifications PhD in crystallography. The EMBL outstation, Hamburg, Germany. Diploma in Biological Sciences. Heidelberg University, Germany.

研究领域

Vitamin B6 Biosynthesis Vitamins are low molecular weight compounds which have to be taken up into our cells in trace amounts, and vitamin deprivation leads to disease. In the body, vitamins often serve as enzymatic cofactors. Studies of their biosynthesis by human pathogens are of particular interest in order to develop specific drugs. The main pathway for de novo vitamin B6 biosynthesis is a recent discovery. We address the architecture of key enzyme complex, PLP synthase and study protein-protein interaction, complex formation, activation of the enzymes and the biosynthesis of the vitamin by the enzyme complex. Protein transport across cell membranes Cell survival critically depends on transport. Metabolic products have to be transferred into and out of the cell, and proteins are secreted. Inside the cell there is transport as well, for example into and out of organelles. These transport phenomena involve transfer across membranes. We study plant chloroplast protein import as one example. Proteins required for photosynthesis are mainly synthesized in the cytosol of plant cells, and thus need to be transported into the organelle. Protein transport is mediated by the Toc-Translocon in the outer chloroplast membrane. The GTPases investigated by us are receptors of protein import. Mycobacterial Adenylyl Cyclases The Mycobacterium tuberculosis genome has 15 open reading frames for class III adenylyl cyclases (ACs). We investigate ACs that respond to environmental pH and lipid composition. The proteins contain a regulatory domain at the N-terminus and a class III cyclase homology domain (CHD) at the C-terminus. Depending on regulatory stimuli, the CHDs dimerise to form the active enzyme. The activated enzymes produce the universal second messenger cAMP from ATP. Reorientation of the catalytic domains on pH change leads to inactivation, while a dimeric structure is retained through interaction of the regulatory domains.

近期论文

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Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis - Rodrigues, Matthew J., Windeisen, Volker, Zhang, Yang, Guédez, Gabriela, Weber, Stefan, Strohmeier, Marco, Hanes, Jeremiah W., Royant, Antoine, Evans, Gwyndaf, Sinning, Irmgard, Ealick, Steven E., Begley, Tadhg P. and Tews, Ivo Published:2017Publication:Nature Chemical BiologyPage Range:1-7doi:10.1038/nchembio.2273PMID:28092359 OX40: structure and function – what questions remain? - Willoughby, Jane, Griffiths, Jordana, Tews, Ivo and Cragg, Mark Published:2017Publication:Molecular ImmunologyVolume:83Page Range:13-22doi:10.1016/j.molimm.2017.01.006 Cholesteryl esters stabilize human CD1c conformations for recognition by self-reactive T cells - Mansour, Salah, Tocheva, Anna S., Cave-Ayland, Christopher, Machelett, Moritz M., Sander, Barbara, Lissin, Nikolai M., Molloy, Peter E., Baird, Mark S., Stübs, Gunthard, Schröder, Nicolas W.J., Schumann, Ralf R., Rademann, Jörg, Postle, Anthony D., Jakobsen, Bent K., Marshall, Ben G., Gosain, Rajendra, Elkington, Paul T, Elliott, Timothy, Skylaris, Chris-Kriton, Essex, Jonathan W., Tews, Ivo and Gadola, Stephan D. Published:2016Publication:Proceedings of the National Academy of SciencesVolume:113, (9)Page Range:E1266-E1275doi:10.1073/pnas.1519246113PMID:26884207 Cholesteryl esters stabilise human CD1c conformations for recognition by self-reactive T cells - Mansour, Salah, Tocheva, Anna, Cave-Ayland, Chris, Machelett, Moritz M., Sander, Barbara, Lissin, Nikolai M., Molloy, Peter E., Baird, Mark S., Stubs, Gunthard, Schroder, Nicolas W.J., Schumann, Ralf R., Rademann, Jorg, Postle, Anthony D., Jakobsen, Bent K., Marshall, Ben G., Gosain, Rajendra, Elkington, Paul, Elliott, Tim, Skylaris, Chris-Kriton, Essex, Jonathan W., Tews, Ivo. and Gadola, Stephan D. Published:2016Publication:Proceedings of the National Academy of SciencesPMID:26884207