Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC

Autor: Samuel, Wagner, Ovidiu Ioan, Pop, Ovidio, Pop, Gert-Jan, Haan, Louise, Baars, Gregory, Koningstein, Mirjam M, Klepsch, Pierre, Genevaux, Joen, Luirink, Jan-Willem, de Gier

Publikováno v: Journal of Biological Chemistry, 283, 17881-1790. American Society for Biochemistry and Molecular Biology Inc.
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2008, pp.17881-17890
Wagner, S, Pop, O I, Haan, G J, Koningstein, G M, Klepsch, M M, Genevaux, P, Luirink, S & de Gier, J-W 2008, ' Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC. ', Journal of Biological Chemistry, vol. 283, pp. 17881-1790 . https://doi.org/10.1074/jbc.M801481200

The polytopic inner membrane protein MalF is a constituent of the MalFGK(2) maltose transport complex in Escherichia coli. We have studied the biogenesis of MalF using a combination of in vivo and in vitro approaches. MalF is targeted via the SRP pat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fcd20e57cc4b3801630fcdb9847fec7
https://doi.org/10.1074/jbc.M801481200

Evidence for Multiple Pathways in the Assembly of the Escherichia coli Maltose Transport Complex

Autor: Beth Traxler, Eliora Gachelet, Kathleen A. Kennedy

Publikováno v: Journal of Biological Chemistry. 279:33290-33297

We used the maltose transport complex MalFGK2 of the Escherichia coli cytoplasmic membrane as a model for the study of the assembly of hetero-oligomeric membrane protein complexes. Analysis of other membrane protein complexes has led to a general mod

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::773ac1d9af09afbc37914101a327ac99
https://doi.org/10.1074/jbc.m403796200

Disulfide Cross-linking Reveals a Site of Stable Interaction between C-terminal Regulatory Domains of the Two MalK Subunits in the Maltose Transport Complex

Autor: Amy L. Davidson, Susmita Samanta, Howard A. Shuman, Moriama Reyes, Jue Chen, Tulin Ayvaz

Publikováno v: Journal of Biological Chemistry. 278:35265-35271

Understanding the structure and function of the ATP-binding cassette (ABC) transporters is very important because defects in ABC transporters lie at the root of several serious diseases including cystic fibrosis. MalK, the ATP-binding cassette of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfd1c407e18c9e153609dc7e56245f56
https://doi.org/10.1074/jbc.m301171200

Demonstration of Conformational Changes Associated with Activation of the Maltose Transport Complex

Autor: Susan Sharma, Amy L. Davidson, Daynene E. Mannering

Publikováno v: Journal of Biological Chemistry. 276:12362-12368

In Escherichia coli, interaction of a periplasmic maltose-binding protein with a membrane-associated ATP-binding cassette transporter stimulates ATP hydrolysis, resulting in translocation of maltose into the cell. The maltose transporter contains two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2bdc4ae41f2e335665202fa2faa9dea
https://doi.org/10.1074/jbc.m011686200

Substrate Transport Activation Is Mediated through Second Periplasmic Loop of Transmembrane Protein MalF in Maltose Transport Complex of Escherichia coli

Autor: Bernd Rupp, Bernd Reif, Erwin Schneider, Tomas Jacso

Publikováno v: The journal of biological chemistry, 287(21): 17040-17049
J. Biol. Chem. 287, 17040-17049 (2012)

In a recent study we described the second periplasmic loop P2 of the transmembrane protein MalF (MalF-P2) of the maltose ATP-binding cassette transporter (MalFGK(2)-E) as an important element in the recognition of substrate by the maltose-binding pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d338233c051839528c5001ac6ed40c01
https://repository.publisso.de/resource/frl:6403020