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
  • BS, 1985, Chemistry, Vassar College

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. Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase. Wittenborn, EC, Cohen, SE, Merrouch, M, Léger, C, Fourmond, V, Dementin, S, Drennan, CL. 2019. J. Biol. Chem. , .
    doi: 10.1074/jbc.RA119.009610PMID:31296570
  2. Solution structure and biochemical characterization of a spare part protein that restores activity to an oxygen-damaged glycyl radical enzyme. Bowman, SEJ, Backman, LRF, Bjork, RE, Andorfer, MC, Yori, S, Caruso, A, Stultz, CM, Drennan, CL. 2019. J. Biol. Inorg. Chem. , .
    doi: 10.1007/s00775-019-01681-2PMID:31250200
  3. X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. Chen, PY, DeColli, AA, Freel Meyers, CL, Drennan, CL. 2019. J. Biol. Chem. 294, 12405-12414.
    doi: 10.1074/jbc.RA119.009321PMID:31239351
  4. DNA repair enzymes ALKBH2, ALKBH3, and AlkB oxidize 5-methylcytosine to 5-hydroxymethylcytosine, 5-formylcytosine and 5-carboxylcytosine in vitro. Bian, K, Lenz, SAP, Tang, Q, Chen, F, Qi, R, Jost, M, Drennan, CL, Essigmann, JM, Wetmore, SD, Li, D et al.. 2019. Nucleic Acids Res. 47, 5522-5529.
    doi: 10.1093/nar/gkz395PMID:31114894
  5. A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes C-C bonds from CO2. Chen, PY, Li, B, Drennan, CL, Elliott, SJ. 2019. Joule 3, 595-611.
    doi: 10.1016/j.joule.2018.12.006PMID:31080943
  6. A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state. Rizzolo, K, Cohen, SE, Weitz, AC, López Muñoz, MM, Hendrich, MP, Drennan, CL, Elliott, SJ. 2019. Nat Commun 10, 1101.
    doi: 10.1038/s41467-019-09020-4PMID:30846684
  7. Crystal Structures of Fumarate Hydratases from Leishmania major in a Complex with Inhibitor 2-Thiomalate. Feliciano, PR, Drennan, CL, Nonato, MC. 2019. ACS Chem. Biol. 14, 266-275.
    doi: 10.1021/acschembio.8b00972PMID:30645090
  8. Crystal structure of AdoMet radical enzyme 7-carboxy-7-deazaguanine synthase from Escherichia coli suggests how modifications near [4Fe-4S] cluster engender flavodoxin specificity. Grell, TAJ, Bell, BN, Nguyen, C, Dowling, DP, Bruender, NA, Bandarian, V, Drennan, CL. 2019. Protein Sci. 28, 202-215.
    doi: 10.1002/pro.3529PMID:30341796
  9. 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
  10. 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. 293, 17349-17361.
    doi: 10.1074/jbc.RA118.005369PMID:30217813
More Publications

Multimedia