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ATP5O — MBP

Text-mined interactions from Literome

Reich-Slotky et al., J Bacteriol 2000 : The detergent-soluble ATPase activity of the complex could be further stimulated by wild-type MBP but not by a signaling-defective mutant MBP
Orelle et al., Proc Natl Acad Sci U S A 2008 : In the intact transporter, closure of the interface coincides not just with the binding of ATP, as seen with isolated nucleotide binding domains, but requires both MBP and ATP, implying that MBP stimulates ATPase activity by promoting the closure of the nucleotide binding interface
Gould et al., Biochemistry 2009 : To gain insight into how MBP regulates the MalFGK ( 2 ) ATPase , we have investigated whether the open or the closed conformation of MBP is responsible for MalFGK ( 2 ) stimulation in the absence of maltose ... These results indicate that stimulation of the MalFGK ( 2 ) ATPase by unliganded MBP does not proceed through a closed conformation and instead must operate through a different mechanism than stimulation by liganded MBP
Gould et al., J Biol Chem 2010 : The ATPase activity of the maltose transporter ( MalFGK ( 2 ) ) is dependent on interactions with the maltose binding protein (MBP)
Cui et al., J Biol Chem 2010 : On the basis of the structure of the MBP-MalFGK ( 2 ) complex in an outward facing conformation ( Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L., and Chen, J. ( 2007 ) Nature 450, 515-521 ), we identified two mutants in transmembrane domains MalF and MalG that generated futile cycling ; although interaction with MBP stimulated the ATPase activity of the transporter, maltose was not transported
Ishii et al., J Biochem 1998 : MBP-DnaJ mediated the replication of the lambda phage in vivo, stimulated the ATPase activity of DnaK and prevented the aggregation of denatured rhodanase, indicating that fusion of MBP to the N-terminal of DnaJ does not affect the functions of DnaJ ... MBP-DnaJ containing Fe and Zn ions, and MBP-DnaJ containing 2 Zn ions stimulated the ATPase activity of DnaK, prevented the aggregation of denatured rhodanase and bound to DNA to similar extents