Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Martin F. Peter"'
Autor:
Martin F. Peter, Jan A. Ruland, Yeojin Kim, Philipp Hendricks, Niels Schneberger, Jan Peter Siebrasse, Gavin H. Thomas, Ulrich Kubitscheck, Gregor Hagelueken
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract The tripartite ATP-independent periplasmic (TRAP) transporters use an extra cytoplasmic substrate binding protein (SBP) to transport a wide variety of substrates in bacteria and archaea. The SBP can adopt an open- or closed state depending o
Externí odkaz:
https://doaj.org/article/b83022bdcbc940eaaa4826707fa4d729
Autor:
Martin F. Peter, Jan A. Ruland, Peer Depping, Niels Schneberger, Emmanuele Severi, Jonas Moecking, Karl Gatterdam, Sarah Tindall, Alexandre Durand, Veronika Heinz, Jan Peter Siebrasse, Paul-Albert Koenig, Matthias Geyer, Christine Ziegler, Ulrich Kubitscheck, Gavin H. Thomas, Gregor Hagelueken
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
Tripartite ATP-independent periplasmic (TRAP) transporters are widespread in bacteria and archaea. Here, the authors used cryo-EM and a range of biophysical techniques to study the structure of function of the sialic acid TRAP transporter HiSiaQM.
Externí odkaz:
https://doaj.org/article/77d7c0c6e18748a0b6f9d495c47f442b
Autor:
Martin F. Peter, Christian Gebhardt, Rebecca Mächtel, Gabriel G. Moya Muñoz, Janin Glaenzer, Alessandra Narducci, Gavin H. Thomas, Thorben Cordes, Gregor Hagelueken
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-19 (2022)
Pulsed electron-electron double resonance spectroscopy (PELDOR/DEER) and single-molecule Förster resonance energy transfer spectroscopy (smFRET) are used to determine conformational changes and probe distances in biological macromolecules. Here the
Externí odkaz:
https://doaj.org/article/c5ec541e9c874f68b54c46726ea64fac
Publikováno v:
BIOspektrum. 29:245-248
TRAP-transporters are widespread in bacteria and archaea and are often responsible for the transport of nutrients or virulence factors in pathogens. They consist of three domains, a substrate-binding protein and two membrane domains. Using cryo-EM, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::395d42880f9f3f59cded0c573ca9add9
https://doi.org/10.1007/s12268-023-1934-7
https://doi.org/10.1007/s12268-023-1934-7
Autor:
Martin F. Peter, Jan A. Ruland, Yeojin Kim, Philipp Hendricks, Jan Peter Siebrasse, Gavin H. Thomas, Ulrich Kubitscheck, Gregor Hagelueken
The tripartite ATP-independent periplasmic (TRAP) transporters use an extra cytoplasmic substrate binding protein (SBP) to transport a wide variety of substrates in bacteria and archaea. The SBP can adopt an ‘open’ or ‘closed’ state depending
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a61f88746c0b0db79aee1e8c07c1b159
https://doi.org/10.1101/2023.03.04.531103
https://doi.org/10.1101/2023.03.04.531103
Autor:
Christophe Rouillon, Niels Schneberger, Haotian Chi, Katja Blumenstock, Stefano Da Vela, Katrin Ackermann, Jonas Moecking, Martin F. Peter, Wolfgang Boenigk, Reinhard Seifert, Bela E. Bode, Jonathan L. Schmid-Burgk, Dmitri Svergun, Matthias Geyer, Malcolm F. White, Gregor Hagelueken
Publikováno v:
Nature
Funding information: M.G. and J.L.S.B. are funded by the Deutsche Forschungsgemeinschaft under Germany’s Excellence Strategy–EXC2151–390873048. M.F.W. acknowledges a European Research Council Advanced Grant (grant number 101018608) and the Chin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4d062fd4abf5ab686d29231fe864680
https://hdl.handle.net/10023/27669
https://hdl.handle.net/10023/27669
Autor:
Christophe Rouillon, Niels Schneberger, Haotian Chi, Martin F. Peter, Matthias Geyer, Wolfgang Boenigk, Reinhard Seifert, Malcolm F. White, Gregor Hagelueken
SummaryCRISPR antiviral defense systems such as the well-known DNA-targeting Cas9- and the more complex RNA-targeting type III systems are widespread in bacteria and archea 1, 2. The type III systems can orchestrate a complex antiviral response that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c19e5a774303fe4a61606f1f9ae34e9c
https://doi.org/10.1101/2021.12.06.471393
https://doi.org/10.1101/2021.12.06.471393
Autor:
Martin F. Peter, Peer Depping, Niels Schneberger, Emmanuele Severi, Karl Gatterdam, Sarah Tindall, Alexandre Durand, Veronika Heinz, Paul-Albert Koenig, Matthias Geyer, Christine Ziegler, Gavin H. Thomas, Gregor Hagelueken
SummaryTripartite ATP-independent periplasmic (TRAP) transporters are widespread in bacteria and archaea and provide important uptake routes for many metabolites 1–3. They consist of three structural domains, a soluble substrate-binding protein (P-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a66b228670338f784790e398c5b5b77
https://doi.org/10.1101/2021.12.03.471092
https://doi.org/10.1101/2021.12.03.471092
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2168
Every membrane protein is involved in close interactions with the lipid environment of cellular membranes. The annular lipids, that are in direct contact with the polypeptide, can in principle be seen as an integral part of its structure, akin to the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a796947908484516578598b1814b7f64
https://pubmed.ncbi.nlm.nih.gov/33582999
https://pubmed.ncbi.nlm.nih.gov/33582999
Autor:
Martin F. Peter, Gregor Hagelueken, Gavin H. Thomas, Marijn de Boer, Janin Glaenzer, Niels Schneberger, Christian Gebhardt, Thorben Cordes
Publikováno v:
Journal of Molecular Biology, 433(3):166756. Academic Press
The pathogens Vibrio cholerae and Haemophilus influenzae use tripartite ATP-independent periplasmic transporters (TRAPs) to scavenge sialic acid from host tissues. They use it as a nutrient or to evade the innate immune system by sialylating surface
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc55921a28523155932bf19e964bcb9f
https://research.rug.nl/en/publications/8247a5f5-fc38-41f2-adcd-6cd7535212e1
https://research.rug.nl/en/publications/8247a5f5-fc38-41f2-adcd-6cd7535212e1