De novo targeting to the cytoplasmic and luminal side of bacterial microcompartments

Autor: Matthew J. Lee, Judith Mantell, Ian R. Brown, Jordan M. Fletcher, Paul Verkade, Richard W. Pickersgill, Derek N. Woolfson, Stefanie Frank, Martin J. Warren

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)

Bacterial microcompartments (BMCs) are protein-bound organelles encapsulating segments of metabolic pathways. Here the authors utilize specific de novo coiled-coil protein-protein interactions to display proteins on the outer or inner surface of BMCs

Externí odkaz: https://doaj.org/article/c4588752a0774db5a65123c4b6546adb

Scaffolding protein GspB/OutB facilitates assembly of the Dickeya dadantii type 2 secretion system by anchoring the outer membrane secretin pore to the inner membrane and to the peptidoglycan cell wall

Autor: Piers Rycroft, Shuang Gu, Shiheng Zhang, Florence Ruaudel, Vladimir E. Shevchik, Xavier Robert, Frédéric Delolme, Lionel Ballut, Richard W. Pickersgill

Publikováno v: mBio
mBio, 2022, 13 (3), pp.e0025322. ⟨10.1128/mbio.00253-22⟩

SummaryThe phytopathogenic proteobacterium Dickeya dadantii secretes an array of plant cell wall degrading enzymes and other virulence factors via the type 2 secretion system (T2SS). T2SSs are widespread among important plant, animal and human bacter

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca384306180d4976a72d5ca8dea9f31a
https://hal.archives-ouvertes.fr/hal-03361905

Structural and functional insights into the pilotin-secretin complex of the type II secretion system.

Autor: Shuang Gu, Saima Rehman, Xiaohui Wang, Vladimir E Shevchik, Richard W Pickersgill

Publikováno v: PLoS Pathogens, Vol 8, Iss 2, p e1002531 (2012)

Gram-negative bacteria secrete virulence factors and assemble fibre structures on their cell surface using specialized secretion systems. Three of these, T2SS, T3SS and T4PS, are characterized by large outer membrane channels formed by proteins calle

Externí odkaz: https://doaj.org/article/8ea1d928c91d4292a9dc3eaf75af9250

De novo targeting to the cytoplasmic and luminal side of bacterial microcompartments

Autor: Derek N. Woolfson, Judith Mantell, Ian R. Brown, Stefanie Frank, Jordan M. Fletcher, Richard W. Pickersgill, Matthew J. Lee, Martin J. Warren, Paul Verkade

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Nature Communications
Lee, M J, Mantell, J, Brown, I R, Fletcher, J M, Verkade, P, Pickersgill, R W, Woolfson, D N, Frank, S & Warren, M J 2018, ' De novo targeting to the cytoplasmic and luminal side of bacterial microcompartments ', Nature Communications, vol. 9, 3413 . https://doi.org/10.1038/s41467-018-05922-x

Bacterial microcompartments, BMCs, are proteinaceous organelles that encase a specific metabolic pathway within a semi-permeable protein shell. Short encapsulation peptides can direct cargo proteins to the lumen of the compartments. However, the fusi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5e55bdc3ae883c0355a709bde184107
https://doi.org/10.1038/s41467-018-05922-x

Structural basis of pyrrole polymerization in human porphobilinogen deaminase

Autor: Paula Pluta, Pietro Roversi, Oscar Millet, Shuang Gu, Richard W. Pickersgill, Adriana L. Rojas, Jonathan B. Cooper, Ganeko Bernardo-Seisdedos

Publikováno v: Biochimica et biophysica acta. General subjects. 1862(9)

Human porphobilinogen deaminase (PBGD), the third enzyme in the heme pathway, catalyzes four times a single reaction to convert porphobilinogen into hydroxymethylbilane. Remarkably, PBGD employs a single active site during the process, with a distinc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37200d9b173016b6054ef9d917017f6c
https://pubmed.ncbi.nlm.nih.gov/29908816