Author

G. Prehna

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· 5

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Research Focus:protein folding & dynamics· 5 Organism:bacteria (other)· 4 Approach:experimental assay· 4 Assay:structural biology· 3 Assay:protein structure· 2 Approach:biophysical modeling· 1 Research Focus:host-pathogen & immune response· 1 Approach:statistical model· 1

Frequent Co-Authors

M. Khajehpour· 2 shared N. Lorente Cobo· 2 shared N. R. Rutbeek· 2 shared A. G. McArthur· 1 shared A. K. C. Brassinga· 1 shared A. Savchenko· 1 shared D. Davidson· 1 shared D. H. Patel· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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2 shared papersBiochemistry

M. Khajehpour

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5 papers

Recent·Most cited

The Streptococcus phage protein paratox is an intrinsically disordered protein.

I. Asakereh, N. R. Rutbeek, M. Singh, D. Davidson, G. Prehna, M. Khajehpour

This paper shows that the phage protein paratox is intrinsically disordered in dilute solution but folds into a globular structure when bound to ComR or in the presence of stabilizing solutes.

Protein Science · May 27, 2024Peer-reviewedBiochemistry

Structural characterization of the Sel1-like repeat protein LceB from Legionella pneumophila

T. V. Penner, N. Lorente Cobo, D. T. Patel, D. H. Patel, A. Savchenko, A. K. C. Brassinga, G. Prehna

This study determines the structure of LceB, a core effector from Legionella pneumophila, revealing its conformational flexibility, self-association, and potential host protein-binding surface.

bioRxiv · Jul 3, 2023Biochemistry

Molecular characterization of the type VI secretion system effector Tlde1a reveals a structurally altered LD-transpeptidase fold

N. Lorente Cobo, S. Sibinelli-Sousa, J. Biboy, W. Vollmer, E. Bayer-Santos, G. Prehna

This study determines the X-ray crystal structure of Tlde1a, a T6SS effector from Salmonella Typhimurium, revealing its unique LD-transpeptidase fold and functional mechanisms.

bioRxiv · Aug 5, 2022Biochemistry

Molecular mechanism of quorum sensing inhibition in Streptococcus by the phage protein paratox

N. R. Rutbeek, H. Rezasoltani, T. R. Patel, M. Khajehpour, G. Prehna

This study elucidates how the phage protein Prx inhibits quorum sensing in Streptococcus pyogenes by inducing conformational changes in the ComR receptor.

bioRxiv · Jun 3, 2021Biochemistry

Structural basis for effector transmembrane domain recognition by type VI secretion system chaperones

S. Ahmad, K. K. Tsang, K. Sachar, D. Quentin, T. M. Tashin, N. P. Bullen, S. Raunser, A. G. McArthur, G. Prehna, J. C. Whitney

The paper identifies a conserved motif in TMD-containing effectors and reveals how Eag chaperones stabilize these domains for T6SS-mediated secretion.

bioRxiv · Oct 28, 2020Biochemistry