My main research area is structural biology and my research interests over postgraduate and postdoctoral years are summarized here:
- 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 York Structural Biology Laboratory (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 (STRUBI) at The Wellcome Trust Centre for Human Genetics, Oxford University, I worked towards solving the structure of influenza RNA-polymerase.
My 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 I work 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.
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.
Crystal structure and functional analysis of human C1ORF123, Siti Nurulnabila A. Rahaman, Jastina Mat Yusop, Zeti-Azura Mohamed-Hussein, Wan Mohd Aizat, Kok Lian Ho, Aik-Hong Teh, Jitka Waterman, Boon Keat Tan, Hwei Ling Tan, Adelicia Yongling L, Ee Sin Chen, Chyan Leong Ng, PubMed 30280012 (September 2018)
Evolutionary Analysis As a Powerful Complement to Energy Calculations for Protein Stabilization, Koen Beerens, Stanislav Mazurenko, Antonin Kunka, Sergio M. Marques, Niels Hansen, Milos Musil, Radka Chaloupkova, Jitka Waterman, Jan Brezovsky, David Bednar, Zbynek Prokop, and Jiri Damborsky, ACS Catal., 2018, 8 (10), pp 9420–9428 (August 2018)
Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative y-butyrolactone receptor protein from Streptomyces fradiae, N. M-Sharif, S. Shaibullah, V. Givajothi, C-S. Tan, K.L. Ho, A-H. Teh, S.N Baharum, J. Waterman, C.L. Ng, Acta Cryst. (2017) F73, 109-115
Cloning, expression, purification, crystallization and X-ray crystallographic analysis of recombinant human C1ORF123 protein, S.N.A. Rahaman, J.M. Yusop, Z. Mohamed-Hussein, K.L. Ho, A-H. Teh, J. Waterman, C.L. Ng, Acta Cryst. (2016) F72, 207-213
Cloning, expression, purification, characterization, crystallization and X-ray crystallographic analysis of recombinant Der f 21 (rDer f 21). S. L. Pang, K. L. Ho, J. Waterman, A.-H. Teh, F. T. Chew and C. L. Ng, Acta Cryst. (2015) F71, 1396-1400.
Industrial Applications at Diamond. E. J. Shotton, L. D. Connor, A. Dias, A. B. Kroner, C. Pizzey, T. Richter, J. Waterman, Synchrotron Radiation News (2014) 27(3), 7-10.
Degradation of phytase by the 6-phytase from Hafnia alvei: a combined structural and solution study. A. Ariza, O. V. Moroz, E. V. Blagova, J. P. Turkenburg, J. Waterman, S. M. Roberts, J. Vind, C. Sjøholm, S. F. Lassen, L. De Maria, V. Glitsoe, L. K. Skov, K. S. Wilson, PLoS One, 8 (2013) 1-13.
An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis. E. Deery, S. Schroeder, A. D. Lawrence, S. L. Taylor, A. Seyedarabi, J. Waterman, K. S. Wilson, D. Brown, M. A. Geeves, M. J. Howard, R. W. Pickersgill, M. J. Warren, Nat Chem Biol, 11 (2012) 933-940.
Diamond: Open for Business. E. J. Shotton, A. Dias, A. B. Kroner, C. Pizzey, J. Waterman, Synchrotron Radiation News (2011) 24(6), 30-33.
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.
Weak activity of haloalkane dehalogenase LinB with 1,2,3-trichloropropane revealed by X-ray crystallography and microcalorimetry, M. Monincová, Z. Prokop, J. Vévodová, Y. Nagata, J. Damborský, App Environ Microbiology, 73 (2007) 1-4.
Crystallization and preliminary structure analysis of CobE, an essential protein of cobalamin (vitamin B12) biosynthesis. J. Vévodová, R. M. Graham, E. Raux, M. J. Warren, K. S. Wilson, Acta Crystallogr F, 61 (2005) 442-4.
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.
Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp. S. Bakhtiar, J. Vévodová, R. Hatti-Kaul, X.-D. Su, Acta Crystallogr D, 59 (2003) 529-531.
Purification, Crystallization and Preliminary X-ray Analysis of a Maize Cytokinin-glucoside-specific b-Glucosidase. J. Vévodová, J. Marek, J. Zouhar, B. Brzobohatý, X.-D. Su, Acta Crystallogr D, 57 (2001) 140-142.
Insights into the Functional Architecture of the Catalytic Center of a Maize Beta-Glucosidase Zm-p60.1 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.