Author

S. Tammam

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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Microbiology· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:bacteria (other)· 4 Research Focus:protein folding & dynamics· 3 Assay:structural biology· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1

Frequent Co-Authors

P. L. Howell· 5 shared L. L. Burrows· 4 shared M. McCallum· 3 shared J. L. Rubinstein· 2 shared A. A. Gheorghita· 1 shared A. Khan· 1 shared E. Kitova· 1 shared G. B. Whitfield· 1 shared

Activity by Year

2016-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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5 shared papersMicrobiology

P. L. Howell

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5 papers

Recent·Most cited

Pseudomonas aeruginosa AlgF is a protein-protein interaction mediator required for acetylation of the alginate exopolysaccharide

K. Low, A. A. Gheorghita, S. Tammam, G. B. Whitfield, Y. E. Li, L. M. Riley, J. Weadge, S. Caldwell, P. A. Chong, M. Walvoort, E. Kitova, J. Klassen, P. L. Howell

This study identifies AlgF as a protein-protein interaction mediator in Pseudomonas aeruginosa that facilitates the formation of an acetylation and export complex for alginate modification.

bioRxiv · Jul 25, 2023Microbiology

CryoEM map of Pseudomonas aeruginosa PilQ enables structural characterization of TsaP

M. McCallum, S. Tammam, J. L. Rubinstein, L. L. Burrows, P. L. Howell

The paper determines the structure of PilQ from Pseudomonas aeruginosa and identifies TsaP as the spoke-forming component, revealing its role in surface-sensing signal transduction.

bioRxiv · May 29, 2020Microbiology

Multiple conformations facilitate PilT function in the type IV pilus

M. McCallum, S. Benlekbir, S. Nguyen, S. Tammam, J. L. Rubinstein, L. L. Burrows, P. L. Howell

The paper determines four X-ray structures of PilT in different conformations and validates their physiological importance through co-evolution analysis and functional studies.

bioRxiv · Jun 15, 2019Microbiology

The type IVa pilus machinery is pre-installed during cell division

T. Carter, R. N. C. Burensuceso, S. Tammam, R. P. Lamers, H. Harvey, P. L. Howell, L. L. Burrows

This study shows that the T4aP machinery is pre-installed at future cell division sites in P. aeruginosa without requiring dedicated peptidoglycan hydrolases.

mBio · Mar 8, 2017Peer-reviewedMicrobiology

The molecular mechanism of the type IVa pilus motors

M. McCallum, S. Tammam, A. Khan, L. L. Burrows, P. L. Howell

This study determines the structure of PilB ATPase domains bound to nucleotides, revealing rotational mechanisms for pilus assembly and disassembly.

bioRxiv · Oct 24, 2016Microbiology