Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. [PDF]
PLoS ONE, 2013 The expression of heteroligomeric protein complexes for structural studies often requires a special coexpression strategy. The reason is that the solubility and proper folding of each subunit of the complex requires physical association with other ...
Mark A Arbing +14 more
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Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2. [PDF]
PLoS ONE, 2012 The maltose transporter MalFGK(2), together with the substrate-binding protein MalE, is one of the best-characterized ABC transporters. In the conventional model, MalE captures maltose in the periplasm and delivers the sugar to the transporter.
Huan Bao, Franck Duong
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Computational analysis of maltose binding protein translocation [PDF]
Philosophical Magazine, 2011 We propose a computational model for the study of maltose binding protein translocation across alpha-hemolysin nanopores. The phenomenological approach simplifies both the pore and the polypeptide chain; however it retains the basic structural protein-like properties of the maltose binding protein by promoting the correct formation of its native key ...
CHINAPPI, MAURO +2 more
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In vitro recombination of non-homologous genes can result in gene fusions that confer a switching phenotype to cells. [PDF]
PLoS ONE, 2011 Regulation of protein activity is central to the complexity of life. The ability to regulate protein activity through exogenously added molecules has biotechnological/biomedical applications and offers tools for basic science.
Richard A Heins +3 more
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Maltoporins and maltose-binding proteins of Yersinia enterocolitica [PDF]
Journal of General Microbiology, 1993 Two components of the Yersinia enterocolitica maltose transport system, maltoporin (OmpM) and an osmotically shockable periplasmic maltose-binding protein (MBP) were identified. The synthesis of OmpM (apparent Mr 43,000) and transport of maltose into cells of Y. enterocolitica were induced by maltose and maltodextrins.
K, Brzostek, H, Heleszko, J, Hrebenda
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Role of Denaturation in Maltose Binding Protein Translocation Dynamics [PDF]
The Journal of Physical Chemistry B, 2012 We present a computational study on the driven transport of the Maltose Binding Protein (MBP) across nanochannels in the framework of coarse-grained modeling. The work is motivated by recent experiments on voltage-driven transport of MBP across nanopores exploring the influence of denaturation on translocation pathways. Our simplified approach allows a
Marco Bacci +3 more
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Crystallization, data collection and data processing of maltose-binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri [PDF]
, 2009 Maltose-binding protein is the periplasmic component of the ABC transporter responsible for the uptake of maltose/maltodextrins. The Xanthomonas axonopodis pv.
Balan, A. +4 more
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Exploration of multi-state conformational dynamics and underlying global functional landscape of maltose binding protein. [PDF]
PLoS Computational Biology, 2012 An increasing number of biological machines have been revealed to have more than two macroscopic states. Quantifying the underlying multiple-basin functional landscape is essential for understanding their functions. However, the present models seem to be
Yong Wang +3 more
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Maltose and maltodextrin utilization by Listeria monocytogenes depend on an inducible ABC transporter which is repressed by glucose. [PDF]
PLoS ONE, 2010 In the environment as well as in the vertebrate intestine, Listeriae have access to complex carbohydrates like maltodextrins. Bacterial exploitation of such compounds requires specific uptake and utilization systems.We could show that Listeria ...
Shubha Gopal +6 more
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Substrate induction and glucose repression of maltose utilization by Streptomyces coelicolor A3(2) is controlled by malR, a member of the lacI-galR family of regulatory genes [PDF]
, 1997 malR of Strepomyces coelicolor A3(2) encodes a homologue of the Lacl/Galr family of repressor proteins, and is divergently transcribed from the malEFG gene cluster, which encodes components of an ATP-dependent transport system that is required for ...
Bibb, M.J. +4 more
core +2 more sources