Jim Naismith

For the sports coach, see James Naismith.
Jim Naismith

Jim Naismith in 2014, picture via the Royal Society
Born James Henderson Naismith
July 26, 1968[1]
Bellshill[1]
Fields
Institutions
Alma mater
Thesis Structural studies of concanavalin A and zinc aldolase (1992)
Doctoral students
Notable awards
Spouse Rachel Middleton[1]
Website
chemistry.st-andrews.ac.uk/staff/jhn/group/

James Henderson Naismith (born 1968) FRS FMedSci is Professor of Chemical Biology and Director of the Biomedical Sciences Research Complex (BSRC) at the University of St Andrews.[1][2][19][20]

Education

Naismith was educated at Hamilton Grammar School.[1] He went on to study at the University of Edinburgh where he was awarded a first class Bachelor of Science degree in Chemistry in 1989. He won a Carnegie Scholarship to work under the supervision of Bill Hunter, John Helliwell and David Garner[21][22] at the University of Manchester where he was awarded a PhD in 1992[23] for research into the chemical structure of Concanavalin A and Zinc aldolase.

Career

Following his PhD, Naismith did postdoctoral research at the University of Texas Southwestern Medical Center as a NATO Fellow in the laboratory of Stephen Sprang.[1][24] He was appointed a Lecturer at the University of St Andrews in 1995 and a Professor in 2001.

Research

Naismith's research investigates:

“ The application of protein structure determination by X-ray crystallography coupled to molecular biology and biochemistry to probe biological mechanisms and to target specific disease pathways. We have ongoing research in
  1. signal transduction
  2. physical basis of protein carbohydrate interactions
  3. pathogenic bacteria glycan assembly, we have cloned and crystallised a number of the enzymes involved in key steps of glycan synthesis in pathogenic bacteria.
  4. viral replication, we are purifying and crystallising a heterodimer crucial to replication of viruses in vivo,
  5. the biosynthesis of unusual natural products.[25]
 ”

His research[26][27][28][29][30][31][32] has been funded by the Biotechnology and Biological Sciences Research Council (BBSRC), the Engineering and Physical Sciences Research Council (EPSRC), the Medical Research Council (MRC),[33] the Wellcome Trust and the European Union.[34]

Awards and honours

Naismith was elected a Fellow of the Royal Society (FRS) in 2014. His nomination reads:

“ Naismith is cited for his stunning structural and chemical dissection of the many proteins involved in natural product recognition, synthesis and export. His work has revealed new paradigms in the recognition of nucleic acids and carbohydrates, unveiled novel chemical mechanisms for enzymatic nucleophilic substitution and addition and provided the first views, both structural and dynamic, of polysaccharide export systems in bacteria. His work is characterised by a synthesis of three-dimensional structural understanding with profound chemical insight.[17] ”

Naismith is also Fellow of the Royal Society of Chemistry (FRSC), the Society of Biology (FSB), the Royal Society of Edinburgh (FRSE), the Academy of Medical Sciences (FMedSci) and an elected member of the European Molecular Biology Organization (EMBO). His nomination for the Academy of Medical Sciences reads:

“ Jim Naismith is Professor of Chemical Biology at St Andrew’s University. He recognised the emerging problem of antibiotic resistance and has devoted his scientific career to the development of new therapeutic compounds and the identification of novel targets specific to microbial pathogens. Highlights include solving the structure and mechanism of a bacterial fluorinating enzyme,[35] determining the mechanism of tryptophan 7-halogenase[36][37] and establishing the structure of an open E. coli mechanosensitive channel. His contributions have been recognised by the Carbohydrate Chemistry Medal of the Royal Society of Chemistry, the Leverhulme Prize in Molecular Biology and the Colworth Medal of Biochemical Society.[18] ”

Personal life

Naismith is married to Rachel Middleton with whom he has one son and one daughter.[1]

References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 NAISMITH, Prof. James Henderson. Who's Who 2014 (online edition via Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc. (subscription required)
  2. ↑ 2.0 2.1 Jim Naismith's publications indexed by Google Scholar, a free service provided by Google
  3. ↑ Boulkeroua, Wassila Abdelli (2013). The application of the fragment-based screening approach to RmlA protein and PA1645 structure (PhD thesis). University of St Andrews.
  4. ↑ Branigan, Emma (2013). Introducing spin labels into proteins to determine their solution conformation by pulsed EPR methods (PhD thesis). University of St Andrews.
  5. ↑ Branigan, E; Pliotas, C; Hagelueken, G; Naismith, J. H. (2013). "Quantification of free cysteines in membrane and soluble proteins using a fluorescent dye and thermal unfolding". Nature protocols 8 (11): 2090–7. doi:10.1038/nprot.2013.128. PMC 3836627. PMID 24091556.
  6. ↑ Huang, Hexian (2013). Regulations of export and chain length of extracellular bacterial polysaccharides (PhD thesis). University of St Andrews.
  7. ↑ Huang, H; Hagelueken, G; Whitfield, C; Naismith, J. H. (2009). "Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae". Acta crystallographica. Section F, Structural biology and crystallization communications 65 (Pt 8): 770–2. doi:10.1107/S1744309109023914. PMC 2720329. PMID 19652335.
  8. ↑ Kowatz, Thomas (2009). Mechanisms of silicate polymerisation, carbohydrate epimerisation and metalloprotease inhibition (PhD thesis). University of St Andrews.
  9. ↑ Kowatz, T; Morrison, J. P.; Tanner, M. E.; Naismith, J. H. (2010). "The crystal structure of the Y140F mutant of ADP-L-glycero-D-manno-heptose 6-epimerase bound to ADP-beta-D-mannose suggests a one base mechanism". Protein science : a publication of the Protein Society 19 (7): 1337–43. doi:10.1002/pro.410. PMC 2974825. PMID 20506248.
  10. ↑ Lou, Hubing (2010). Structural and functional studies of bacterial outer membrane proteins (PhD thesis). University of St Andrews.
  11. ↑ Lou, H; Chen, M; Black, S. S.; Bushell, S. R.; Ceccarelli, M; Mach, T; Beis, K; Low, A. S.; Bamford, V. A.; Booth, I. R.; Bayley, H; Naismith, J. H. (2011). "Altered antibiotic transport in OmpC mutants isolated from a series of clinical strains of multi-drug resistant E. Coli". PloS one 6 (10): e25825. doi:10.1371/journal.pone.0025825. PMC 3203869. PMID 22053181.
  12. ↑ Reeks, Judith (2013). Structural studies of CRISPR-associated proteins (PhD thesis). University of St Andrews.
  13. ↑ Reeks, J; Graham, S; Anderson, L; Liu, H; White, M. F.; Naismith, J. H. (2013). "Structure of the archaeal Cascade subunit Csa5: Relating the small subunits of CRISPR effector complexes". RNA biology 10 (5): 762–9. doi:10.4161/rna.23854. PMC 3737334. PMID 23846216.
  14. ↑ Schmelz, Stefan (2010). Adenylate forming enzymes involved in NRPS-independent siderophore biosynthesis (PhD thesis). University of St Andrews.
  15. ↑ Schmelz, S; Botting, C. H.; Song, L; Kadi, N. F.; Challis, G. L.; Naismith, J. H. (2011). "Structural basis for acyl acceptor specificity in the achromobactin biosynthetic enzyme AcsD". Journal of molecular biology 412 (3): 495–504. doi:10.1016/j.jmb.2011.07.059. PMC 3323832. PMID 21835184.
  16. ↑ Yan, Xuan (2011). Structural analysis of the potential therapeutic targets from specific genes in Methicillin-resistant Staphylococcus aureus (MRSA) (PhD thesis). University of St Andrews.
  17. ↑ 17.0 17.1 "Professor James Naismith FMedSci FRS". London: The Royal Society. Archived from the original on 2014-08-14.
  18. ↑ 18.0 18.1 Professor James Naismith FRS FRSE FMedSci, Academy of Medical Sciences
  19. ↑ List of publications from Microsoft Academic Search
  20. ↑ Jim Naismith's publications indexed by the Scopus bibliographic database, a service provided by Elsevier.
  21. ↑ Professor Jim Naismith biography, via Diamond Light Source
  22. ↑ Jim Naismith, Scientific Advisory Board via the Manchester Institute of Biotechnology
  23. ↑ Naismith, Jim (1992). Structural studies of Concanavalin A and zinc aldolase (PhD thesis). University of Manchester. (subscription required)
  24. ↑ Naismith, J. H.; Sprang, S. R. (1995). "Tumor necrosis factor receptor superfamily". Journal of inflammation 47 (1–2): 1–7. PMID 8913924.
  25. ↑ The Naismith Structural Biology Group: Changing the world, one structure at a time…, University of St Andrews
  26. ↑ Idriss, H. T.; Naismith, J. H. (2000). "TNF alpha and the TNF receptor superfamily: Structure-function relationship(s)". Microscopy research and technique 50 (3): 184–95. doi:10.1002/1097-0029(20000801)50:3<184::AID-JEMT2>3.0.CO;2-H. PMID 10891884.
  27. ↑ Blankenfeldt, W; Asuncion, M; Lam, J. S.; Naismith, J. H. (2000). "The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA)". The EMBO journal 19 (24): 6652–63. doi:10.1093/emboj/19.24.6652. PMC 305900. PMID 11118200.
  28. ↑ Sanders, D. A.; Staines, A. G.; McMahon, S. A.; McNeil, M. R.; Whitfield, C; Naismith, J. H. (2001). "UDP-galactopyranose mutase has a novel structure and mechanism". Nature structural biology 8 (10): 858–63. doi:10.1038/nsb1001-858. PMID 11573090.
  29. ↑ Naismith, J. H.; Sprang, S. R. (1998). "Modularity in the TNF-receptor family". Trends in biochemical sciences 23 (2): 74–9. PMID 9538693.
  30. ↑ Tatham, M. H.; Jaffray, E; Vaughan, O. A.; Desterro, J. M.; Botting, C. H.; Naismith, J. H.; Hay, R. T. (2001). "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9". The Journal of biological chemistry 276 (38): 35368–74. doi:10.1074/jbc.M104214200. PMID 11451954.
  31. ↑ Naismith, J. H.; Field, R. A. (1996). "Structural basis of trimannoside recognition by concanavalin A". The Journal of biological chemistry 271 (2): 972–6. doi:10.1074/jbc.271.2.972. PMID 8557713.
  32. ↑ Dong, C; Beis, K; Nesper, J; Brunkan-Lamontagne, A. L.; Clarke, B. R.; Whitfield, C; Naismith, J. H. (2006). "Wza the translocon for E. Coli capsular polysaccharides defines a new class of membrane protein". Nature 444 (7116): 226–9. doi:10.1038/nature05267. PMC 3315050. PMID 17086202.
  33. ↑ UK Government research grants awarded to James Henderson Naismith, via Research Councils UK
  34. ↑ "Major honour for St Andrews scientist Jim Naismith". University of St Andrews. 2014-05-01. Archived from the original on 2014-08-15.
  35. ↑ Dong, C; Huang, F; Deng, H; Schaffrath, C; Spencer, J. B.; O'Hagan, D; Naismith, J. H. (2004). "Crystal structure and mechanism of a bacterial fluorinating enzyme". Nature 427 (6974): 561–5. doi:10.1038/nature02280. PMID 14765200.
  36. ↑ Dong, C; Kotzsch, A; Dorward, M; Van Pée, K. H.; Naismith, J. H. (2004). "Crystallization and X-ray diffraction of a halogenating enzyme, tryptophan 7-halogenase, from Pseudomonas fluorescens". Acta crystallographica. Section D, Biological crystallography 60 (Pt 8): 1438–40. doi:10.1107/S0907444904012521. PMID 15272170.
  37. ↑ Dong, C; Flecks, S; Unversucht, S; Haupt, C; Van Pée, K. H.; Naismith, J. H. (2005). "Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination". Science 309 (5744): 2216–9. doi:10.1126/science.1116510. PMC 3315827. PMID 16195462.