| Coupling between ATP hydrolysis and protein conformational change in maltose transporter MalK has been described. | Coupling between ATP hydrolysis and protein conformational change in maltose transporter.
Lv X, Liu H, Chen H, Gong H. | 06/24/2017 |
| Data indicate that MalFGK2 transporter is comprised of two membrane proteins, MalF and MalG, and the nucleotide-binding domain, which controls the conformation of MalFG, is composed of the homodimeric MalK subunit. | Formation of a Chloride-conducting State in the Maltose ATP-binding Cassette (ABC) Transporter.
Carlson ML, Bao H, Duong F., Free PMC Article | 12/17/2016 |
| Data suggest that the binding and conformational change of maltose transporter (MalFGK2) may provide some insights into the understanding of the mechanism of ABC transporters. | Allosteric transitions of the maltose transporter studied by an elastic network model.
Li CH, Yang YX, Su JG, Liu B, Tan JJ, Zhang XY, Wang CX. | 06/4/2016 |
| The water-mediated entropic force is important for ATP-induced conformational changes of nucleotide-binding domains in MalK. | ATP-induced conformational changes of nucleotide-binding domains in an ABC transporter. Importance of the water-mediated entropic force.
Hayashi T, Chiba S, Kaneta Y, Furuta T, Sakurai M. | 10/10/2015 |
| Escherichia coli maltose binding protein has inhibitory effects on beta-amyloid aggregation and cytotoxicity | The inhibitory effects of Escherichia coli maltose binding protein on β-amyloid aggregation and cytotoxicity.
Sharoar MG, Shahnawaz M, Islam MI, Ramasamy VS, Shin SY, Park IS. | 11/16/2013 |
| The molecular entity that interacts with MalT is not free MalK, but the maltose transporter, MalFGK(2) , which sequesters MalT to the membrane. | The ABC transporter MalFGK(2) sequesters the MalT transcription factor at the membrane in the absence of cognate substrate.
Richet E, Davidson AL, Joly N., Free PMC Article | 01/12/2013 |
| using x-ray crystallography, study captured the maltose transporter in an intermediate step between the inward- and outward-facing states | Crystal structure of the maltose transporter in a pretranslocation intermediate state.
Oldham ML, Chen J. | 06/25/2011 |
| substrate availability is communicated from MalE to the MalK dimer via extracytoplasmic loops of MalFG | Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK(2)) from Escherichia coli/Salmonella during the transport cycle.
Daus ML, Berendt S, Wuttge S, Schneider E. | 01/21/2010 |
| 2.8-A crystal structure of the intact maltose transporter in complex with the maltose-binding protein, maltose and ATP | Crystal structure of a catalytic intermediate of the maltose transporter.
Oldham ML, Khare D, Quiocho FA, Davidson AL, Chen J. | 01/21/2010 |
| ATP-driven MalK dimer closure and reopening are crucial steps in the translocation cycle of the intact maltose transporter MalFGK2 | ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2).
Daus ML, Grote M, Müller P, Doebber M, Herrmann A, Steinhoff HJ, Dassa E, Schneider E. | 01/21/2010 |
| Data suggest that the MalT/MalK interaction might involve two distinct contact sites on each partner. | Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK.
Richet E, Joly N, Danot O. | 01/21/2010 |