By combining X-ray crystallography, cryo-electron microscopy and other biophysical methods, the goal of the Drennan lab is to “visualize” molecular processes by obtaining snapshots of enzymes in action.

Office

Phone

617-253-5622

cdrennan@mit.edu

Administrative Assistant

Read Schusky

Assistant Phone

(617) 258-7851

Lab Website

Catherine L. Drennan

Professor of Biology and Chemistry
Investigator and Professor, Howard Hughes Medical Institute

Research Areas

Office

68-680

Phone

617-253-5622

cdrennan@mit.edu

Administrative Assistant

Read Schusky

Assistant Phone

(617) 258-7851

Lab Website

The Drennan laboratory seeks to understand how Nature harnesses and re-directs the reactivity of enzyme metallocenters in order to perform challenging reactions. By combining X-ray crystallography with other biophysical methods, their goal is to “visualize” molecular processes by obtaining snapshots of enzymes in action.

Key Publications

See all on the Drennan Group Website

Disruption of an Oligomeric Interface Prevents Allosteric Inhibition of Escherichia coli class Ia Ribonucleotide Reductase

Chen‡, P.Y.-T., Funk‡, M.A., Brignole, E.J., and Drennan*, C.L. (2018). J. Biol. Chem. 293, 10404-10412

Full Text on PubMed

3.3-Å Resolution Cryo-EM Structure of Human Ribonucleotide Reductase with Substrate and Allosteric Regulators Bound

Brignole ‡, E.J, Tsai ‡, K.-L., Chittuluru, J., Li, H., Aye, Y., Penczek, P.A., Stubbe*, J., Drennan*, C.L., and Asturias*, F. (2018). eLife 7, e31502. PMCID: PMC5819950

Full Text at PubMed

Biochemical and Structural Characterization of a Schiff Base in the Radical-Mediated Biosynthesis of 4-Demethylwyosine by TYW1

Grell‡, T.A.J., Young‡, A.P., Drennan*, C.L., and Bandarian*, V. (2018). J. Am. Chem. Soc. 140, 6842-6852. PMCID: PMC5994729

Full Text at PubMed

Binding Site for Coenzyme A Revealed in the structure of Pyruvate:Ferredoxin Oxidoreducatase from Moorella thermoacetica

Chen, P.Y.-T., Aman, H., Can, M., Ragsdale, S.W., and Drennan*, C.L. (2018). Proc. Natl. Acad. Sci. U.S.A. 115, 3846-3851. PMCID: PMC5899475

Full Text at PubMed

Structural Basis for Methylphosphonate Biosynthesis

Born, D.A. ‡, Ulrich, E.C. ‡, Ju, K.-S., Peck, S.C., van der Donk, W.A.*, and Drennan, C.L.* (2017). Science 358, 1336-1339. 29217579. PMID: 29217579. DOI:10.1126/science.aao3435 ‡The authors contributed equally to this work. *Corresponding Authors

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A B12-dependent radical SAM enzyme involved in Oxetanocin-A biosynthesis

Bridwell-Rabb, J. ‡, Zhong, A. ‡, Sun, H.G., Drennan, C.L.*, and Liu, H.-w.* (2017). Nature 544, 322-326. PMCID: PMC5398914 ‡The authors contributed equally to this work. *Corresponding Authors

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Molecular Basis for Allosteric Specificity Regulation in Class Ia Ribonucleotide Reductase from Escherichia coli

Zimanyi, C.M., Chen, P.Y.-T., Kang, G., Funk, M.A., and Drennan*, C.L. (2016). eLife 5, e07141. PMCID: PMC4728125

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Crystallographic Snapshots of Sulfur Insertion by Lipoyl Synthase

McLaughlin, M.I., Lanz, N.D., Goldman, P.J., Lee, K.-H., Booker, S.J., Drennan, C.L. (2016). Proc. Natl. Acad. Sci. U.S.A. 113, 9446-9450. PMCID: PMC5003258

Full Text at PubMed

Molecular Basis of C–N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase

Bodea‡, S., Funk‡, M.A., Balskus*, E.P., and Drennan*, C.L. (2016). Cell Chem. Biol. 23, 1206-1216. PMCID: PMC5493019

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Structural Basis for Gene Regulation by a B12-dependent Photoreceptor

Jost, M., Fernández-Zapata, J., Polanco, M.C., Ortiz-Guerrero, J.M., Chen, P. Y.-T., Kang, G., Padmanabhan. S., Elías-Arnanz, M., and Drennan, C.L. (2015). Nature 526, 536-41. PMCID: PMC4634937

Full Text at PubMed