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Gerwald Jogl, PhD

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Gerwald Jogl

Title: Associate Professor of Biology
Department: Molecular Biology, Cell Biology, & Biochemistry

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Overview | Research | Grants/Awards | Teaching | Publications

We use X-ray crystallography as our main research tool (together with biochemical and biophysical approaches) to study the structure and function of proteins and macromolecular complexes.

The overall goal of our research is to understand the molecular mechanism of antibiotic resistance caused by mutations in bacterial ribosomes and to evaluate the contribution of post-transcriptional rRNA modifications for ribosome function and antibiotic resistance.


  • Post-doctoral Research Associate with Liang Tong, Columbia University

  • Ph.D. in Chemistry, Karl Franzens Universität Graz, Austria, with Christoph Kratky: "X-ray and Neutron Diffraction Studies of B12 Coenzymes in Free and Enzyme Bound State"

  • M.Sc. in Chemistry, Karl Franzens Universität Graz, Austria, with Christoph Kratky: "Solid State Reactions in Cob(II)alamin Crystals"


Karl Franzens University Graz, Austria

Research Description

Bacterial ribosomes are a major drug target for treating infectious diseases, and more than half of all antibiotics interfere with protein synthesis. The ribosome is a large and complex cellular machine that translates genetic information into proteins, which in turn carry out most of the metabolic functions required for cellular life. Because this translation from nucleic acids into amino acids is a fundamental process, ribosomes are present in all forms of life. Many antibiotic drugs (eg. streptomycin, the first drug to treat tuberculosis) bind selectively to bacterial ribosomes and disrupt protein synthesis, ultimately killing the disease causing bacteria. Mutations within ribosomes that disrupt antibiotic binding sites or enable ribosomes to function in the presence of these antibiotic compounds are one cause for the emergence of resistance against ribosome targeting antibiotics. Structural studies of ribosomes carrying these antibiotic-resistance mutations are a powerful tool for understanding the molecular mechanism of resistance. This, in turn, can provide new leads for the development of new or modified compounds, which are active against resistant pathogens.
Our studies of the ribosome are carried out in a close collaboration with Drs. Albert Dahlberg and Steven Gregory here at Brown University. We use the bacterium Thermus thermophilus as a model system because this organism is amenable to both genetic and structural studies. Ribosomal mutations that result in resistance to streptomycin or a number of other antibiotic compounds have been identified and characterized in the laboratories of Dr. Dahlberg and Dr. Gregory. Because of the powerful combination of genetic expertise in the Dahlberg and Gregory laboratories and of crystallographic expertise in our laboratory, we are in a unique position to systematically examine mutant ribosome structures.
With ongoing experiments, we currently explore two broad areas of research. For the first area, we investigate the mechanism of antibiotic resistance and the impact of mutations and post-transcriptional modifications on ribosome structure and function. For the second area, we study ribosome modifying enzymes and other multi-specific enzymes to understand the molecular basis for multi-specific enzymatic activity.


M.Sc. Thesis Award of the Austrian Chemical Society 1994


American Crystallographic Association
American Society for Biochemistry and Molecular Biology
American Association for the Advancement of Sciences
RNA Society

Funded Research

  • NIH R01GM094157-01, 9/15/10 - 8/31/15,
    Structural robustness of ribosome functional centers
    MPI grant with Dr. Steven Gregory

  • 2008: Brown University Salomon Faculty Research Award

  • 2006: Medical Research Award, Rhode Island Foundation
    01/06 $10,000

  • 2006: Brown University Research Seed Fund (with Rebecca Page)
    Structural Biology and Function of Macromolecular Complexes: Using Light Scattering to Initiate the Establishment of a Brown University Facility for State-of-the-Art Protein Biophysical Characterization
    02/2006 $53,000

Courses Taught

  • Current Topics in Biochemistry and Molecular Biology (BI0221)
  • Current Topics in Biochemistry and Molecular Biology (BI0220)
  • Independent Research (BI0195)
  • Introductory Biochemistry (BI0028)

View My Full Publication List in pdf format

Selected Publications

  • Demirci H, Murphy IV FM, Murphy E, Gregory S, Dahlberg AE, Jogl G*; A structural basis for streptomycin-induced misreading of the genetic code. Nature Comms. 10.1038/ncomms2364 (2013).(2013)
  • Larsen LH, Rasmussen A, Giessing AM, Jogl G*, Kirpekar F*; Identification and characterization of the Thermus thermophilus m5C methyltransferase modifying 23S rRNA base C1942. J. Biol. Chem. 287, 27593-27600 (2012).(2012)
  • Li H and Jogl G*; Crystal structure of decaprenylphosphoryl-β-D-ribose 2'-epimerase from Mycobacterium smegmatis. Proteins, 81(3), 538-543 (2012).(2012)
  • Jogl G, Wang X, Mason SA, Kovalevsky A, Mustyakimov M, Fisher Z, Hoffman C, Kratky C, Langan P; High-resolution neutron crystallographic studies of the hydration of the coenzyme cob(II)alamin. Acta Cryst. D 67, 584-591 (2011).(2011)
  • Demirci H, Larsen HGL, Hansen T, Rasmussen A, Cadambi A, Gregory ST, Kirpekar F, Jogl G; Multi-site specific 16S rRNA methyltransferase RsmF from Thermus thermophilus. RNA 16, 1584-1596 (2010)(2010)
  • Demirci H, Murphy IV FM, Belardinelli R, Kelley AC, Ramakrishnan V, Gregory ST, Dahlberg AE, Jogl G; Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function. RNA 16, 2319-2324.(2010)
  • Demirci H, Belardinelli R, Seri E, Gregory ST, Gualerzi C, Dahlberg AE, Jogl G; Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine. J. Mol. Biol. 388, 271-282 (2009).(2009)
  • Li H and Jogl G; Structural and biochemical studies of TIGAR (TP53-Induced Glycolysis and Apoptosis Regulator). J. Biol. Chem. 284, 1748-1754 (2009).(2009)
  • Gregory ST, Demirci H, Belardinelli R, Monshupanee T, Gualerzi C, Dahlberg AE, Jogl G; Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG. RNA 15, 1693-1704 (2009).(2009)
  • Demirci H, Gregory S, Dahlberg AE, Jogl G; Multiple site trimethylation of ribosomal protein L11 by the PrmA methyltransferase. Structure, 16, 1059-1066 (2008).(2008)
  • Demirci H, Gregory S, Dahlberg AE, Jogl G; Crystal structure of the Thermus thermophilus 16S rRNA methyltransferase RsmC in complex with cofactor and substrate guanosine. J. Biol. Chem. 283, 26548-26556 (2008).(2008)
  • Demirci H, Gregory S, Dahlberg A, Jogl G; Recognition of Ribosomal Protein L11 by the Protein Trimethyltransferase PrmA. EMBO J., 26, 567-577 (2007).(2007)
  • Li H and Jogl G; Crystal Structure of the Zinc-binding Transport Protein ZnuA from Escherichia coli Reveals an Unexpected Variation in Metal Coordination. JMB, 368, 1358-1366 (2007).(2007)
  • You Z, Omura S, Ikeda H, Cane DE, Jogl G; Crystal Structure of the Non-heme Iron Dioxygenase PtlH in Penatlenolactone Biosynthesis. J. Biol. Chem. 282, 36552-36560 (2007).(2007)
  • Holmes W and Jogl G; Crystal Structure of Inositol Phosphate Multikinase 2 and Implications for Substrate Specificity. J. Biol. Chem., 281, 38109-38116 (2006)(2006)
  • Jogl G, Hsiao Y, Tong L: Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity. J. Biol. Chem., 280, 738-744 (2005).(2005)
  • Jogl G, Tong, L: Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP. Biochemistry, 43, 1425-1431 (2004).(2004)
  • Jogl G, Tong, L: Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport. Cell, 112, 113-122 (2003).(2003)
  • Jogl G, Rozovsky S, McDermott AE, Tong, L: Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2Å resolution. Proc. Natl. Acad. Sci. USA, 100, 1, 50-55 (2003).(2003)