Catherine Drennan

Catherine Drennan

Professor of Biology and Chemistry; Investigator and Professor, Howard Hughes Medical Institute; MacVicar Faculty Fellow

Catherine Drennan takes “snapshots” of metalloenzymes using crystallography and/or cryo-electron microscopy.

617-253-5622

Phone

68-680

Office

cdrennan@mit.edu

Email

Lab Website
Read Schusky

Assistant

617-258-7851

Assistant Phone

Education

PhD 1995, University of Michigan

Research Summary

We use X-ray crystallography to investigate the structure and function of enzymes that are medically important in environmental remediation. We are particularly interested in metalloprotein biochemistry, and in the role of conformational change in catalysis.

Awards

  • Howard Hughes Medical Institute, HHMI Investigator, 2008
  • Howard Hughes Medical Institute, HHMI Professor, 2006

Key Publications

  1. A B12-dependent radical SAM enzyme involved in oxetanocin A biosynthesis. Bridwell-Rabb, J, Zhong, A, Sun, HG, Drennan, CL, Liu, HW. 2017. Nature 544, 322-326.
    doi: 10.1038/nature21689PMID:28346939
  2. Crystallographic snapshots of sulfur insertion by lipoyl synthase. McLaughlin, MI, Lanz, ND, Goldman, PJ, Lee, KH, Booker, SJ, Drennan, CL. 2016. Proc. Natl. Acad. Sci. U.S.A. 113, 9446-50.
    doi: 10.1073/pnas.1602486113PMID:27506792
  3. Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli. Zimanyi, CM, Chen, PY, Kang, G, Funk, MA, Drennan, CL. 2016. Elife 5, e07141.
    doi: 10.7554/eLife.07141PMID:26754917
  4. Structural basis for gene regulation by a B12-dependent photoreceptor. Jost, M, Fernández-Zapata, J, Polanco, MC, Ortiz-Guerrero, JM, Chen, PY, Kang, G, Padmanabhan, S, Elías-Arnanz, M, Drennan, CL. 2015. Nature 526, 536-41.
    doi: 10.1038/nature14950PMID:26416754
  5. Visualizing molecular juggling within a B12-dependent methyltransferase complex. Kung, Y, Ando, N, Doukov, TI, Blasiak, LC, Bender, G, Seravalli, J, Ragsdale, SW, Drennan, CL. 2012. Nature 484, 265-9.
    doi: 10.1038/nature10916PMID:22419154

Recent Publications

  1. Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase. Wittenborn, EC, Merrouch, M, Ueda, C, Fradale, L, Léger, C, Fourmond, V, Pandelia, ME, Dementin, S, Drennan, CL. 2018. Elife 7, .
    doi: 10.7554/eLife.39451PMID:30277213
  2. Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. Grell, TAJ, Kincannon, WM, Bruender, NA, Blaesi, EJ, Krebs, C, Bandarian, V, Drennan, CL. 2018. J. Biol. Chem. , .
    doi: 10.1074/jbc.RA118.005369PMID:30217813
  3. A Rich Man, Poor Man Story of S-Adenosylmethionine and Cobalamin Revisited. Bridwell-Rabb, J, Grell, TAJ, Drennan, CL. 2018. Annu. Rev. Biochem. 87, 555-584.
    doi: 10.1146/annurev-biochem-062917-012500PMID:29925255
  4. Isonitrile Formation by a Non-Heme Iron(II)-Dependent Oxidase/Decarboxylase. Harris, NC, Born, DA, Cai, W, Huang, Y, Martin, J, Khalaf, R, Drennan, CL, Zhang, W. 2018. Angew. Chem. Int. Ed. Engl. 57, 9707-9710.
    doi: 10.1002/anie.201804307PMID:29906336
  5. Disruption of an oligomeric interface prevents allosteric inhibition of Escherichia coli class Ia ribonucleotide reductase. Chen, PY, Funk, MA, Brignole, EJ, Drennan, CL. 2018. J. Biol. Chem. 293, 10404-10412.
    doi: 10.1074/jbc.RA118.002569PMID:29700111
  6. Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica. Chen, PY, Aman, H, Can, M, Ragsdale, SW, Drennan, CL. 2018. Proc. Natl. Acad. Sci. U.S.A. 115, 3846-3851.
    doi: 10.1073/pnas.1722329115PMID:29581263
  7. 3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound. Brignole, EJ, Tsai, KL, Chittuluru, J, Li, H, Aye, Y, Penczek, PA, Stubbe, J, Drennan, CL, Asturias, F. 2018. Elife 7, .
    doi: 10.7554/eLife.31502PMID:29460780
  8. Structural basis for methylphosphonate biosynthesis. Born, DA, Ulrich, EC, Ju, KS, Peck, SC, van der Donk, WA, Drennan, CL. 2017. Science 358, 1336-1339.
    doi: 10.1126/science.aao3435PMID:29217579
  9. New tricks for the glycyl radical enzyme family. Backman, LRF, Funk, MA, Dawson, CD, Drennan, CL. 2017. Crit. Rev. Biochem. Mol. Biol. 52, 674-695.
    doi: 10.1080/10409238.2017.1373741PMID:28901199
  10. Monovalent Cation Activation of the Radical SAM Enzyme Pyruvate Formate-Lyase Activating Enzyme. Shisler, KA, Hutcheson, RU, Horitani, M, Duschene, KS, Crain, AV, Byer, AS, Shepard, EM, Rasmussen, A, Yang, J, Broderick, WE et al.. 2017. J. Am. Chem. Soc. 139, 11803-11813.
    doi: 10.1021/jacs.7b04883PMID:28768413
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