Embedded Files
2022 - present
Cartwright, M.; Jha, R. K.; and Smith, A. T. Structure and mechanism of aminoacyl-tRNA-protein L/F- and R-transferases. J. Mol. Biol. 2025, 437, 169210.
Paredes, A.; Singh, H.; Hull, M.; Greene, D.#; Northrup, A. J.#; Brown, J. B.; Chacón, K. N.; Patrauchan, M. A.; and Smith, A. T. The Response Regulator BqsR/CarR Controls Ferrous Iron (Fe2+) Acquisition in Pseudomonas aeruginosa. bioRxiv. 2025, DOI: 10.1101/2025.04.12.648518
Paredes, A.; Iheacho, C.#; Chacón, K. N.; and Smith, A. T. The Pseudomonas aeruginosa membrane histidine kinase BqsS/CarS directly senses environmental ferrous iron (Fe2+). bioRxiv. 2025, DOI: 10.1101/2025.04.06.647434
Lee, M.; Armstrong, C. M.; and Smith, A. T. Characterization of intact FeoB in a lipid bilayer using styrene-maleic acid (SMA) copolymers. BBA-Biomembranes. 2025, 1867, 184404.
Cartwright, M.; Parakra, R.; Oduwole, A.#; Zhang, F.; Deredge, D. J.; and Smith, A. T. Identification of an intrinsically disordered region (IDR) in arginyltransferase 1 (ATE1). Biochemistry. 2024, 63, 3236-3249.
Lee, M.; Magante, K.#; Gómez-Garzón, C.; Payne, S. M.; and Smith, A. T. Structural determinants of Vibrio cholerae FeoB nucleotide promiscuity. J. Biol. Chem. 2024, 300, 107663 and bioRxiv. 2024, DOI: 10.1101/2024.05.22.595361
Paredes, A.; Iheacho, C.#; and Smith, A. T. Metal messengers: communication in the bacterial world through transition-metal-sensing two-component systems. Biochemistry. 2023, 62, 2339-2357.
Van, V.; Brown, J. B.; O'Shea, C. R.; Rosenbach, H.; Mohamed, I.#; Ejimogu, N.-E.#; Bui, T. S.#; Szalai, V. A.; Chacón, K. N.; Span, I.; Zhang, F.; and Smith, A. T. Iron-sulfur clusters are involved in post-translational arginylation. Nature Communications. 2023, 14, 458, DOI: 0.1038/s41467-023-36158-z and bioRxiv. 2021, DOI: 10.1101/2021.04.13.439645
Van, V. and Smith, A. T. Reconstitution of the arginyltransferase (ATE1) iron-sulfur cluster. In: Kashina, A. S. (ed.) Protein Arginylation: Methods and Protocols. Methods in Molecular Biology, 2023, 2620, 209-217.
Cartwright, M.; Van, V.; and Smith, A. T. The preparation of recombinant arginyltransferase 1 (ATE1) for biophysical characterization. Methods Enzymol. 2023, 678, 235-254.
Van, V.; Ejimogu, N.-E.#; Bui, T. S.#; and Smith, A. T. The structure of Saccharomyces cerevisiae arginyltransferase 1 (ATE1). J. Mol. Biol. 2022, 434, 167816 and bioRxiv. 2022, DOI: 10.1101/2022.07.20.500667
Sestok, A. E.; O'Sullivan, S. M.#; and Smith A. T. A general protocol for the expression and purification of the intact transmembrane transporter FeoB. BBA-Biomembranes. 2022, 1864, 183973.
Sestok, A. E.; Brown, J. B.; Obi, J. O.; O'Sullivan, S. M.#; Garcin, E. D.; Deredge, D. J.; and Smith A. T. A fusion of the Bacteroides fragilis ferrous iron import proteins reveals a role for FeoA in stabilizing GTP-bound FeoB. J. Biol. Chem. 2022, 298, 101808.
Brown, J. B.; Lee, M. A.; and Smith, A. T. The structure of Vibrio chloerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain. J. Biol. Inorg. Chem. 2022, 27, 485-495 and bioRxiv. 2022, DOI: 10.1101/2022.02.26.482101
Sestok, A. E.; Lee, M.; and Smith, A. T. Prokaryotic ferrous iron uptake: exploiting pools of reduced iron across multiple microbial environments. In: Hurst, C.J. (ed) Microbial Metabolism of Metals and Metalloids. Advances in Environmental Microbiology. 2022, 10, 299-357. Springer, Cham. DOI: 10.1007/978-3-030-97185-4_12
Smith, A. T. Protein arginylation is regulated during SARS-CoV-2 infection. Rapid Reviews: COVID-19. 2022, DOI: 10.1162/2e3983f5.63d125d7
2016 - 2021
Brown, J. B.; Lee, M. A.; and Smith, A. T. Ins and outs: recent advancements in membrane protein-mediated prokaryotic ferrous iron transport. Biochemistry. 2021, 60, 3277-3291.
Sestok, A. E.; Brown, J. B.; Obi, J. O.; O'Sullivan, S. M.#; Garcin, E. D.; Deredge, D. J.; and Smith A. T. Biochemical and structural characterization of the fused Bacteroides fragilis NFeoAB domain reveals a role for FeoA. bioRxiv. 2021. DOI: https://doi.org/10.1101/2021.09.29.462438
Sánchez-Osuna, M.; Cortés, P.; Lee, M.; Smith, A. T.; Barbé, J.; and Erill, I. Non-canonical LexA proteins regulate the SOS response in the Bacteroidetes. Nucleic Acids Res. 2021, 49, 11050-11066.
Article promoted by The Conversation (10.19.2021)
Cain, T. J. and Smith, A. T. Ferric iron reductases and their contribution to unicellular ferrous iron uptake. J. Inorg. Biochem. 2021, 218, 11407, 1-9.
Van, V. and Smith, A. T. ATE1-mediated post-translational arginylation is an essential regulator of eukaryotic cellular homeostasis. ACS Chem. Biol. 2020, 15, 3073-3085.
Smith, A. T.; Linkous, R. O.#; Max, N. J.; Sestok, A. E.; Szalai, V.A.; and Chacón, K. N. The FeoC [4Fe-4S] cluster is redox-active and rapidly oxygen-sensitive. Biochemistry. 2019, 58, 4935-4949.
Smith, A. T.; Linkous, R. O.#; Max, N. J.; Sestok, A. E.; Szalai, V.A.; and Chacón, K. N. Escherichia coli FeoC binds a redox-active, rapidly oxygen-sensitive [4Fe-4S] cluster. ChemRxiv. 2019. DOI: https://doi.org/10.26434/chemrxiv.8411408.v1
Linkous, R. O.#; Sestok, A. E.; and Smith, A. T. The crystal structure of Klebsiella pneumoniae FeoA reveals a site for protein-protein interactions. Proteins. 2019, 87, 897-903 and bioRxiv. 2019. DOI: https://doi.org/10.1101/514059
Sestok, A. E.; Linkous, R. O.#; and Smith, A. T. Toward a mechanistic understanding of Feo-mediated ferrous iron uptake. Metallomics. 2018, 10, 887-898.†
Smith, A. T. and Sestok, A. E. Expression and purification of functionally active ferrous iron transporter FeoB from Klebsiella pneumoniae. Protein Expr. Purif. 2018, 142, 1-7.
Smith, A. T.; Ross, M. O.; Hoffman, B. M.; Rosenzweig, A. C. Metal selectivity of a Cd-, Co-, and Zn-transporting P1B-type ATPase. Biochemistry. 2017, 56, 85-95.
Hines, J. P.; Smith, A. T.; Jacob, J. P.; Lukat-Rodgers, G. S.; Barr, I.; Rodgers, K. R.; Guo, F.; Burstyn, J. N. CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity. J. Biol. Inorg. Chem. 2016, 21, 1021-1035.
†Highlighted as the journal cover.
#Indicates undergraduate author.
Prior to 2016
Smith, A. T.; Barupala, D.; Stemmler, T.L.; Rosenzweig, A. C. A new metal binding domain involved in cadmium, cobalt and zinc transport. Nature Chem. Biol. 2015, 11, 678-674.
Kathman, S.; Span, I.; Smith, A. T.; Xu, Z.; Zhan, J.; Rosenzweig, A. C.; Statsyuk, A. Discovery and structural characterization of covalent inhibitors of Nedd4-1 ubiquitin ligase processivity J. Am. Chem. Soc. 2015, 137, 12442-12445.
Smith, A. T. * ; Pazicni, S. * ; Marvin, K. A. * ; Stevens, D. J.; Freeman, K. M.; Burstyn, J. N. Functional divergence of heme-thiolate proteins: a classification based on spectroscopic attributes. Chem. Rev. 2015, 115, 2532-2558.
Smith, A. T., Smith, K.P., and Rosenzweig, A. C. Diversity of the metal-transporting P1B-type ATPases. J. Biol. Inorg. Chem. 2014, 19, 947-960.
Smith, A. T.; Marvin, K. A.; Freeman, K. M.; Kerby, R. L.; Roberts, G. P.; Burstyn, J. N. Identification of Cys94 as the distal ligand to the Fe(III) heme in the transcriptional regulator RcoM-2 from Burkholderia xenovorans. J. Biol. Inorg. Chem. 2012, 17, 1071-1082.
Smith, A. T.; Su, Y.; Stevens, D. J.; Majtan, T.; Kraus, J. P.; Burstyn, J. N. The effect of the disease-causing R266K mutation on the heme and PLP environments of the human enzyme cystathionine β-synthase. Biochemistry. 2012, 51, 6360-6370.
Barr, I.; Smith, A. T.; Chen, Y.; Senturia, R.; Burstyn, J. N.; Guo, F. Ferric, not ferrous, heme activates RNA-binding protein DGCR8 for primary microRNA processing. Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 1919-1924.
Barr, I.; Smith, A. T.; Senturia, R.; Chen, Y.; Burstyn, J. N.; Guo, F. DiGeorge Critical Region 8 (DGCR8) is a double-cysteine ligated heme protein. J. Biol. Chem.2011, 286, 16716-16725.
Smith, A. T.; Majtan, T.; Freeman, K. M.; Su, Y.; Kraus, J. P.; Burstyn, J. N. Cobalt cystathionine β-synthase: a cobalt-substituted heme protein with a unique thiolate ligation motif. Inorg. Chem. 2011, 50, 4417-4427.
Matjan, T.; Freeman, K. M.; Smith, A. T.; Burstyn, J. N.; Kraus, J. P. Purification and characterization of cystathionine β-synthase bearing cobalt protoporphyrin. Arch. Biochem. Biophys. 2011, 508, 25-30.
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