Thomas Bohl, Ph.D.

Thomas Bohl, Ph.D.
Postdoctoral fellow, Huilin Li Laboratory


Dr. Thomas Bohl earned their B.A. in biochemistry and molecular biology from the College of Wooster and their Ph.D. in biochemistry, molecular biology and biophysics from University of Minnesota. Their graduate work focused on two enzymes (LpxB and LpxH) that synthesize the membrane anchor of lipopolysaccharide (LPS) in Gram-negative bacteria. Their research also gave them extensive experience in X-ray crystallography. In 2018, they joined the laboratory of Dr. Huilin Li at Van Andel Institute as a postdoctoral fellow.


Current research focus

I am working to structurally characterize the complexes of the glycosyltransferases (GTs) that synthesize the initial oligosaccharide transferred to Asn in glycoproteins. The oligosaccharide is attached as proteins are secreted into the endoplasmic reticulum, and these GTs are bound to the ER membrane with the early GTs acting on the cytoplasmic side and the late GTs acting on the luminal side. These GTs are highly conserved in eukaryotes, and glycosylation is important for protein folding, stability and secretion. Mutations in the genes encoding these GTs cause so-called congenital defects of glycosylation in humans, which can cause severe disease phenotypes. I will be utilizing cryo-electron microscopy to structurally characterize these membrane-bound complexes.

Education & Training

Ph.D. in biochemistry, molecular biology and biophysics, University of Minnesota–Twin Cities (Advisor: Professor Hideki Aihara)
Thesis: Structural studies of two enzymes in the Raetz pathway of lipid A synthesis, LpxB and LpxH

B.A. in biochemistry and molecular biology, The College of Wooster

Awards & External Funding

Ross A. Gortner Award, University of Minnesota (2018)

Sisodia-Williams Prize in Biochemistry, College of Wooster (2012)

John W. Chittum Prize in Chemistry, College of Wooster (2011)


To view a list of selected publications click below.

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Bohl T, Shi K, Lee J, Aihara H. 2018. Crystal structure of the lipid A disaccharide synthase LpxB from Escherichia coli. Nat Commun 9:377.

Bohl T, Ieong P, Lee J, Lee T, Kankanala J, Shi K, Demir O, Kurahashi K, Amaro R, Wang Z, Aihara H. 2018. The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem 293:7969–7981.

Bohl T, Aihara H. 2018. Current progress in the structural and biochemical characterization of proteins involved in the assembly of lipopolysaccharide. Int J Microbiol.

Shi K, Bohl T, Park J, Zasada A, Malik S, Banerjee S, Tran V, Li N, Yin Z, Kurniawan F,  Orellana K, Aihara H. 2018. T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction. Nucleic Acids Res.


Read More

Bohl T, Shi K, Lee J, Aihara H. 2017. Crystal structure of lipid A disaccharide synthase (LpxB) from E. coli (Poster); Gordon Research Seminar: Proteins (Holderness, New Hampshire)

Bohl T, Shi K, Lee J, Aihara H. 2017. X-ray Crystallography of LpxB: An Enzyme in the Lipid A Synthesis Pathway (Lecture); American Crystallographic Association 2017 Meeting: Etter Symposium (New Orleans, Louisiana)