Author

A. T. Smith

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 7 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Organism:bacteria (other)· 4 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 3 Research Focus:protein structure prediction· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1

Frequent Co-Authors

B. Vezina· 3 shared J. B. Brown· 3 shared A. E. Sestok· 2 shared A. Golneshin· 2 shared B. H. A. Rehm· 2 shared M. C. Gor· 2 shared N.-E. Ejimogu· 2 shared T. S. Bui· 2 shared

Activity by Year

2019-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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3 shared papersBiochemistry

B. Vezina

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

The structure of arginyltransferase 1 (ATE1)

V. Van, N.-E. Ejimogu, T. S. Bui, A. T. Smith

This study determines the crystal structure of ScATE1, revealing its bilobed architecture, catalytic site, and regulatory [Fe-S] cluster connectivity, providing insights into eukaryotic post-translational arginylation mechanisms.

bioRxiv · Jul 20, 2022 · PreprintBiochemistry

The structure of Vibrio cholerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain

J. B. Brown, M. A. Lee, A. T. Smith

This paper determines the NMR structure of VcFeoC, revealing a truncated winged-β-sheet without the cluster-binding domain, and shows its interaction with VcFeoB.

bioRxiv · Feb 26, 2022Biochemistry

Biochemical and structural characterization of the fused Bacteroides fragilis NFeoAB domain reveals a role for FeoA

A. E. Sestok, J. B. Brown, J. O. Obi, S. M. O'Sullivan, E. D. Garcin, D. Deredge, A. T. Smith

This study characterizes the Bacteroides fragilis NFeoAB fusion protein, revealing FeoA's role in stabilizing the GTP-bound form of FeoB through nucleotide-dependent interactions.

bioRxiv · Sep 29, 2021 · PreprintBiochemistry

Iron-sulfur clusters are involved in post-translational arginylation

V. Van, J. B. Brown, H. Rosenbach, I. Mohamed, N.-E. Ejimogu, T. S. Bui, V. A. Szalai, K. N. Chacon, I. Span, A. T. Smith

This study identifies an iron-sulfur cluster in ATE1 enzymes that regulates arginylation efficacy and links it to oxidative stress sensing via the N-degron pathway.

bioRxiv · Apr 13, 2021Biochemistry

Are specialised ABC transporters responsible for the circularisation of type I circular bacteriocins?

B. Vezina, B. H. A. Rehm, A. T. Smith

The paper investigates whether specialised ABC transporters are responsible for the circularisation of type I circular bacteriocins but has been withdrawn due to pending verification.

bioRxiv · Dec 23, 2020 · PreprintMicrobiology

Crystal structure and site-directed mutagenesis of circular bacteriocin plantacyclin B21AG reveals cationic and aromatic residues important for antimicrobial activity

M. C. Gor, B. Vezina, R. M. McMahon, G. J. King, S. Panjikar, B. H. A. Rehm, J. L. Martin, A. T. Smith

The paper determines the crystal structure of plantacyclin B21AG and identifies key cationic and aromatic residues critical for its antimicrobial activity through site-directed mutagenesis.

bioRxiv · Jul 2, 2020Biochemistry

Cloning and functional expression of a food-grade circular bacteriocin, plantacyclin B21AG, in probiotic Lactobacillus plantarum WCFS1

M.-C. Gor, A. Golneshin, T. T. H. Van, R. J. Moore, A. T. Smith

The paper clones and functionally expresses a circular bacteriocin, plantacyclin B21AG, in the probiotic Lactobacillus plantarum WCFS1, demonstrating antimicrobial activity.

bioRxiv · Apr 23, 2020Microbiology

Discovery and characterisation of novel circular bacteriocin plantacyclin B21AG from Lactobacillus plantarum B21

A. Golneshin, M. C. Gor, B. Vezina, N. Williamson, T. T. H. Van, B. K. May, A. T. Smith

This study identifies and characterizes plantacyclin B21AG, a novel circular bacteriocin from Lactobacillus plantarum B21, highlighting its antimicrobial properties and biosynthetic machinery.

bioRxiv · Apr 10, 2020Biochemistry

The crystal structure of Klebsiella pneumoniae FeoA reveals a site for protein-protein interactions

R. O. Linkous, A. E. Sestok, A. T. Smith

The paper determines the crystal structure of Klebsiella pneumoniae FeoA, revealing an SH3-like domain that mediates protein-protein interactions with FeoB through conformational changes.

bioRxiv · Jan 8, 2019Biochemistry