Vanderbilt University School of Medicine

Iverson, Tina M. , Ph.D.
Associate Professor of Pharmacology
Associate Professor of Biochemistry

Lab Url:

Phone Number: 615 322 7817


Iverson, Tina's picture

Office Address   Mailing Address

460 Robinson Research Building

460 RRB; Department of Pharmacology Vanderbilt University Medical Center 37232-6600

Research Keywords
x-ray crystallography, signaling, receptors, enzymes,Enzyme action,Ion transport,Membrane,Molecular medicine,Protein Structure,Receptor,Signal transduction,Structural Biology

Research Specialty
The structural basis for molecular recognition

Research Description
Cells must be able to recognize and respond to rapid changes in their environments. These molecular recognition events occur when membrane-spanning receptors physically interact with a stimulus on the outside of the cell and initiate the activation of downstream effectors. To reveal how this information about the extracellular milieu is converted into a cellular response, we are performing x-ray crystallographic analysis of several model systems to determine the atomic details of proteins interactions important for molecular recognition.
Disparate proteins form transient complexes across the membrane during signal propagation, yet these complexes likely share common mechanisms of signaling mediated by changes in conformation, electrostatics, or dynamics. While challenging, the determination of the architecture of these complexes is required for understanding how biological signals are transmitted across a membrane. The research in the Iverson laboratory uses several model systems to investigate these transmembrane signaling processes, and is concurrently working to develop methods for membrane protein crystallography.

Iverson, TM. Catalytic mechanisms of complex II enzymes: a structural perspective. Biochim Biophys Acta, 1827(5), 648-57, 2013.

Seo, HS, Minasov, G, Seepersaud, R, Doran, KS, Dubrovska, I, Shuvalova, L, Anderson, WF, Iverson, TM, Sullam, PM. Characterization of Fibrinogen Binding by Glycoproteins Srr1 and Srr2 of Streptococcus agalactiae. J Biol Chem, 288(50), 35982-96, 2013.

Singh, PK, Sarwar, M, Maklashina, E, Kotlyar, V, Rajagukguk, S, Tomasiak, TM, Cecchini, G, Iverson, TM. Plasticity of the quinone-binding site of the complex II homolog quinol:fumarate reductase. J Biol Chem, 288(34), 24293-301, 2013.

Thaker, TM, Tanabe, M, Fowler, ML, Preininger, AM, Ingram-Smith, C, Smith, KS, Iverson, TM. Crystal structures of acetate kinases from the eukaryotic pathogens Entamoeba histolytica and Cryptococcus neoformans. J Struct Biol, 181(2), 185-9, 2013.

Vishnivetskiy, SA, Chen, Q, Palazzo, MC, Brooks, EK, Altenbach, C, Iverson, TM, Hubbell, WL, Gurevich, VV. Engineering visual arrestin-1 with special functional characteristics. J Biol Chem, 288(5), 3394-405, 2013.

Zhuang, T, Chen, Q, Cho, MK, Vishnivetskiy, SA, Iverson, TM, Gurevich, VV, Sanders, CR. Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc Natl Acad Sci U S A, 110(3), 942-7, 2013.

Iverson, TM, Maklashina, E, Cecchini, G. Structural basis for malfunction in complex II. J Biol Chem, 287(42), 35430-8, 2012.

Iverson, TM, Panosian, TD, Birmingham, WR, Nannemann, DP, Bachmann, BO. Molecular Differences between a Mutase and a Phosphatase: Investigations of the Activation Step in Bacillus cereus Phosphopentomutase. Biochemistry, 51(9), 1964-1975, 2012.

Thaker, TM, Kaya, AI, Preininger, AM, Hamm, HE, Iverson, TM. Allosteric mechanisms of g protein-coupled receptor signaling: a structural perspective. Methods Mol Biol, 796, 133-74, 2012.

Kaya, AI, Thaker, TM, Preininger, AM, Iverson, TM, Hamm, HE. Coupling Efficiency of Rhodopsin and Transducin in Bicelles. Biochemistry, 15(50), 3193-203, 2011. PMCID:3040645

Kuchtey, J, Olson, LM, Rinkoski, T, Mackay, EO, Iverson, TM, Gelatt, KN, Haines, JL, Kuchtey, RW. Mapping of the Disease Locus and Identification of ADAMTS10 As a Candidate Gene in a Canine Model of Primary Open Angle Glaucoma. PLoS Genet, 7(2), e1001306, 2011. PMCID:3040645

Panosian, TD, Nannemann, DP, Watkins, GR, Phelan, VV, McDonald, WH, Wadzinski, BE, Bachmann, BO, Iverson, TM. Bacillus cereus Phosphopentomutase Is an Alkaline Phosphatase Family Member That Exhibits an Altered Entry Point into the Catalytic Cycle. J Biol Chem, 286(10), 8043-54, 2011.

Pyburn, TM, Bensing, BA, Xiong, YQ, Melancon, BJ, Tomasiak, TM, Ward, NJ, Yankovskaya, V, Oliver, KM, Cecchini, G, Sulikowski, GA, Tyska, MJ, Sullam, PM, Iverson, TM. A structural model for binding of the serine-rich repeat adhesin GspB to host carbohydrate receptors. PLoS Pathog, 7(7), e1002112, 2011. PMCID:3131266

Tomasiak, TM, Archuleta, TL, Andrell, J, Lunz-Chavez, C, Davis, TA, Sarwar, M, Ham, AJ, McDonald, WH, Yankovskaya, V, Stern, HA, Johnston, JN, McLashina, E, Cecchini, G, Iverson, TM. Geometric restraint drives on- and off-pathway catalysis by the Escherichia coli menaquinol:fumarate reductase. J Biol Chem, 286(4), 3047-3056, 2011.

Panosian, TD, Nannemann, DP, Bachmann, BO, Iverson, TM. Crystallization and preliminary X-ray analysis of a phosphopentomutase from Bacillus cereus. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66(Pt 7), 811-4, 2010.

Pyburn, TM, Yankovskaya, V, Bensing, BA, Cecchini, G, Sullam, PM, Iverson, TM. Purification, crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding region of the Streptococcus gordonii adhesin GspB. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66(Pt 11), 1503-7, 2010.

Tanabe, M, Nimigean, CM, Iverson, TM. Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proc Natl Acad Sci U S A, 107(15), 6811-6, 2010.

Vey, JL, Al-Mestarihi, A, Hu, Y, Funk, MA, Bachmann, BO, Iverson, TM. Structure and mechanism of ORF36, an amino sugar oxidizing enzyme in everninomicin biosynthesis . Biochemistry, 49(43), 9306-17, 2010.

Adler, DH, Phillips, JA, Cogan, JD, Iverson, TM, Schnetz-Boutaud, N, Stein, JA, Brenner, DA, Milne, GL, Morrow, JD, Boutaud, O, Oates, JA. The enteropathy of prostaglandin deficiency. J Gastroenterol, 44 Suppl 19, 1-7, 2009.

Preininger, AM, Funk, MA, Oldham, WM, Meier, SM, Johnston, CA, Adhikary, S, Kimple, AJ, Siderovski, DP, Hamm, HE, Iverson, TM. Helix dipole movement and conformational variability contribute to allosteric GDP release in Galphai subunits. Biochemistry, 48(12), 2630-42, 2009.

Tanabe, M, Iverson, TM. Expression, purification and preliminary X-ray analysis of the Neisseria meningitidis outer membrane protein PorB. Acta Crystallogr Sect F Struct Biol Cryst Commun, 65(Pt 10), 996-1000, 2009.

Thompson, AN, Kim, I, Panosian, TD, Iverson, TM, Allen, TW, Nimigean, CM. Mechanism of potassium-channel selectivity revealed by Na(+) and Li(+) binding sites within the KcsA pore. Nat Struct Mol Biol, 16(12), 1317-24, 2009.

Adler, DH, Cogan, JD, Phillips, JA, Schnetz-Boutaud, N, Milne, GL, Iverson, T, Stein, JA, Brenner, DA, Morrow, JD, Boutaud, O, Oates, JA. Inherited human cPLA(2alpha) deficiency is associated with impaired eicosanoid biosynthesis, small intestinal ulceration, and platelet dysfunction. J Clin Invest, 118(6), 2121-31, 2008. PMCID:2350426

Tomasiak, TM, Maklashina, E, Cecchini, G, Iverson, TM. A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II. J Biol Chem, 283(22), 15460-8, 2008. PMCID:2397489

Iverson, TM. Evolution and unique bioenergetic mechanisms in oxygenic photosynthesis. Curr Opin Chem Biol, 10(2), 91-100, 2006.

Maklashina, E, Iverson, TM, Sher, Y, Kotlyar, V, Andrell, J, Mirza, O, Hudson, JM, Armstrong, FA, Rothery, RA, Weiner, JH, Cecchini, G. Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain. J Biol Chem, 281(16), 11357-11365, 2006.

Ferreira, KN, Iverson, TM, Maghlaoui, K, Barber, J, Iwata, S. Architecture of the photosynthetic oxygen-evolving center. Science, 303(5665), 1831-8, 2004.

Cecchini, G, Maklashina, E, Yankovskaya, V, Iverson, TM, Iwata, S. Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases. FEBS Lett, 545(1), 31-8, 2003.

Doukov, TI, Iverson, TM, Seravalli, J, Ragsdale, SW, Drennan, CL. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science, 298(5593), 567-72, 2002.

Iverson, TM, Luna-Chavez, C, Croal, LR, Cecchini, G, Rees, DC. Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J Biol Chem, 277(18), 16124-30, 2002.

Iyer, R, Iverson, TM, Accardi, A, Miller, C. A biological role for prokaryotic ClC chloride channels. Nature, 419(6908), 715-8, 2002.

Iverson, TM, Arciero, DM, Hooper, AB, Rees, DC. High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea. J Biol Inorg Chem, 6(4), 390-7, 2001.

Strop, P, Smith, K S, Iverson, T M, Ferry, J G, Rees, D C. Crystal structure of the 'cab'-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum. J Biol Chem, 276(13), 10299-305, 2001.

Iverson, T M, Luna-Chavez, C, Schroder, I, Cecchini, G, Rees, D C. Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex. Curr Opin Struct Biol, 10(4), 448-55, 2000.

Iverson, TM, Alber, BE, Kisker, C, Ferry, JG, Rees, DC. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry, 39(31), 9222-31, 2000.

Luna-Chavez, C, Iverson, T M, Rees, D C, Cecchini, G. Overexpression, purification, and crystallization of the membrane-bound fumarate reductase from Escherichia coli. Protein Expr Purif, 19(1), 188-96, 2000.

Iverson, T M, Luna-Chavez, C, Cecchini, G, Rees, D C. Structure of the Escherichia coli fumarate reductase respiratory complex. Science, 284(5422), 1961-6, 1999.

Iverson, TM, Arciero, DM, Hsu, BT, Logan, MS, Hooper, AB, Rees, DC. Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea. Nat Struct Biol, 5(11), 1005-12, 1998.

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