Jitka Waterman
Industrial Liaison Office
Jitka Waterman (née Vévodová) is an Industrial Liaison Scientist at Diamond Light Source with research expertise in the area of Structural Biology and Macromolecular X-ray Crystallography. She joined the Industrial Liaison Office in November 2011 after working as a post-doctoral research associate at the Division of Stuctural Biology at the University of Oxford. Previously, after a PhD in Biophysics at the Masaryk University in the Czech Republic and Molecular Biophysics at the Lund University, Sweden, she worked in the Structural Biology Laboratory at The University of York.
Jitka’s role as an Industrial Liaison Scientist is to assist industrial users with diffraction data collection on the MX beamlines and further establish and maintain collaboration with Diamond’s industrial partners. Together with other members of the Industrial Liaison team, she works towards gaining maximal benefit from accessibility of complementary techniques such as Small Angle X-ray Scattering (SAXS) or Circular Dichroism (CD) to provide complex information about biological systems.
Email: Jitka Waterman
Tel: +44 (0) 1235 778233
Industrial Liaison Office
Key research areas:
Structural biology, macromolecular x-ray crystallography, SAXS, CDResearch Interests:
Structural biology is concerned with structural and functional relationships in macromolecular systems, especially proteins and nucleic acids. Within the field, protein crystallography is the most important method for the determination of novel structures as well as rational drug design. This method, and its combination with complementary techniques, allows a deep understanding of biological processes and systems.
During my years of postdoctoral research, I studied various macromolecules. The haloalkane dehalogenase LinB from S. paucimobilis is an enzyme involved in the degradation of the important environmental pollutant γ-hexachlorocyclohexane. The enzyme hydrolyzes a broad range of halogenated cyclic and aliphatic compounds and could be a useful starting material for the development of a new biocatalyst.
The maize (Zea mays) beta-glucosidase Zm-p60.1 has been implicated to be one of the key enzymes involved in the regulation of plant development by releasing active phytohomornes, cytokinins, from cytokinin-O-glucosides, their inactive storage and transport forms. Elucidation of aglycone specificity in β-glucosidases is a key prerequisite toward uncovering their precise role(s) in biological processes that involve glucosylation and deglucosylation as regulatory elements. At the same time, the ability to modulate specificity in β-glucosidases holds considerable promise in terms of their biotechnological applications.
At YSBL, I contributed to the clarification of Cobalamin biosynthesis in Pseudomonas sp. by solving the structures of two essential proteins involved in this pathway. P. denitrificans S-adenosyl-L-methionine-dependent uroporphyrinogen III is a branchpoint enzyme that plays a key role in the biosynthesis of modified tetrapyrroles by controlling flux to compounds such as vitamin B(12) and sirohaem, and catalysing the transformation of uroporphyrinogen III into precorrin-2. CobE from P. aeruginosa is a component of the aerobic Cobalamin biosynthetic pathway although its precise role has not been elucidated. The enzyme has a novel topology and was proposed to be essential for the extrusion of the "C2" unit of the porphyrin ring.
The intracellular subtilisin proteases are the only known members of the important and ubiquitous subtilisin family that function exclusively within the cell, constituting a major component of the degradome in many Gram-positive bacteria. The dimeric ISP from B. clausii reveals novel structural features which are unique to this subtilisin family and provides a potential novel regulatory mechanism of intrinsic proteolytic activity.
I gained a great deal of experience whilst participating on an industrial cooperative project with Novozymes.
At the Structural Biology Laboratory at The Wellcome Trust Centre for Human Genetics, Oxford University (STRUBI), I worked towards solving the structure of influenza RNA-polymerase.
Selected Publications:
- Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family.J. Vévodová, M. Gamble, G. Künze, A. Ariza, E. Dodson, D. D. Jones, K. S. Wilson, Structure, 18 (2010), 744-755.
- Structural and mutational analyses of the interaction between the barley alpha-amylase/subtilisin inhibitor and the subtilisin savinase reveal a novel mode of inhibition P.O. Micheelsen, J. Vévodová, L. De Maria, P.R. Ostergaard, E.P. Friis, K.S. Wilson, M. Skjøt, J Mol Biol 380 (2008) 681-90.
- Structure/function studies on a S-adenosyl-L-methionine dependent uroporphyrinogen-III- C-methyltransferase (SUMT), a key regulatory enzyme of the tetrapyrrole biosynthesis. J. Vévodová, R. M. Graham, E. Raux, H. L. Schubert, D. I. Roper, A. A. Brindley, A. I. Scott, C. A. Roessner, N. P. J. Stamford, M. E. Stroupe, E. D. Getzoff, M. J. Warren, K. S. Wilson J Mol Biol. 344 (2004) 419-33.
- Insights into the Functional Architecture of the Catalytic Center of a Maize Beta-Glucosidase Zm-p60. J. Vévodová, J. Zouhar, J. Marek, J. Damborský, X.-D. Su, B. Brzobohatý, Plant Physiology, 127 (2001) 973-985.
- Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26.J. Marek, J. Vévodová, I. Kutá-Smatanová, Y. Nagata, L. A. Svensson, J. Newman, M. Takagi, J. Damborský, Biochemistry, 39 (2000) 14082-14086.