Welcome to the Iverson Lab

Research in the Iverson laboratory focuses on the basis for information encoding in proteins, which may manifest as molecular recognition and cellular communication. We use several model systems to understand information encoding. Research projects in our lab provide complementary information on how proteins encode information into their structures under very different biological settings. This information encoding helps bioenergetics proteins act as primordial signal scaffolds, allows mammalian signaling proteins to use conformations to select between possible outcomes, and allows hosts to recognize pathogens, and vice versa.

Iverson Lab

Singh P K, Sharma P, Afanzar O, Goldfarb M H , Maklashina E, Eisenbach M, Cecchini G, Iverson T M, CryoEM structures reveal how the bacterial flagellum rotates and switches direction Nature Microbiology. 2024 Apr 17

Singh P K , Cecchini G , Nakagawa T , Iverson T M , CryoEM structure of a post-assembly MS-ring reveals plasticity in stoichiometry and conformation PloS one. 2023 May 19; 18 (5). e0285343

Sharma P, Maklashina E, Cecchini G, Iverson TM. Crystal structure of an assembly intermediate of respiratory Complex II. Nature communications. 2018 Jan 18;9(1). 274 p.

Bensing, B.A., Loukachevitch, L.V., McCulloch, K.M., Yu ,H., Vann, K.R., Wawrzak, Z., Anderson, S., Chen, X., Sullam, P.M., Iverson, T.M. (2016) Structural Basis for Sialoglycan Binding by the Streptococcus sanguinis SrpA Adhesin. J. Biol. Chem. 291(14):7230-40.

McCulloch, K.M., McCranie, E.K., Smith, J.A., Sarwar, M., Mathieu, J.L., Gitschlag, B.L., Du, Y., Bachmann, B.O., and Iverson, T.M. (2015) Oxidative cyclizations in orthosomycin biosynthesis expand the known chemistry of an oxygenase superfamily. Proc Natl Acad Sci USA. 112(37):11547-52.

Chen, Q., Perry, N.A., Vishnivetskiy, S.A., Berndt, S., Gilbert, N.C., Zhuo, Y., Singh, P.K., Tholen, J., Ohi, M.D., Gurevich, E.V., Brautigam, C.A., Klug, C.S., Gurevich, V.V., Iverson, T.M. (2017) Structural basis of arrestin-3 activation and signaling. Nat Commun. 2017 Nov 10;8(1):1427.

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Singh P K, Sharma P, Afanzar O, Goldfarb M H , Maklashina E, Eisenbach M, Cecchini G, Iverson T M, CryoEM structures reveal how the bacterial flagellum rotates and switches direction Nature Microbiology. 2024 Apr 17

Singh P K , Cecchini G , Nakagawa T , Iverson T M , CryoEM structure of a post-assembly MS-ring reveals plasticity in stoichiometry and conformation PloS one. 2023 May 19; 18 (5). e0285343

Sharma P, Maklashina E, Cecchini G, Iverson TM. Crystal structure of an assembly intermediate of respiratory Complex II. Nature communications. 2018 Jan 18;9(1). 274 p.

Bensing, B.A., Loukachevitch, L.V., McCulloch, K.M., Yu ,H., Vann, K.R., Wawrzak, Z., Anderson, S., Chen, X., Sullam, P.M., Iverson, T.M. (2016) Structural Basis for Sialoglycan Binding by the Streptococcus sanguinis SrpA Adhesin. J. Biol. Chem. 291(14):7230-40.

McCulloch, K.M., McCranie, E.K., Smith, J.A., Sarwar, M., Mathieu, J.L., Gitschlag, B.L., Du, Y., Bachmann, B.O., and Iverson, T.M. (2015) Oxidative cyclizations in orthosomycin biosynthesis expand the known chemistry of an oxygenase superfamily. Proc Natl Acad Sci USA. 112(37):11547-52.

Chen, Q., Perry, N.A., Vishnivetskiy, S.A., Berndt, S., Gilbert, N.C., Zhuo, Y., Singh, P.K., Tholen, J., Ohi, M.D., Gurevich, E.V., Brautigam, C.A., Klug, C.S., Gurevich, V.V., Iverson, T.M. (2017) Structural basis of arrestin-3 activation and signaling. Nat Commun. 2017 Nov 10;8(1):1427.