scholarly journals Binding Protein-Dependent Uptake of Maltose into Cells via an ATP-Binding Cassette Transporter

EcoSal Plus ◽  
2010 ◽  
Vol 4 (1) ◽  
Author(s):  
Amy L. Davidson ◽  
Frances Joan D. Alvarez
Keyword(s):  
Binding Protein ◽  
Atp Binding ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

scholarly journals The MalF P2 Loop of the ATP-Binding Cassette Transporter MalFGK2 from Escherichia coli and Salmonella enterica Serovar Typhimurium Interacts with Maltose Binding Protein (MalE) throughout the Catalytic Cycle

2008 ◽  
Vol 191 (3) ◽  
pp. 754-761 ◽  
Author(s):  
Martin L. Daus ◽  
Mathias Grote ◽  
Erwin Schneider
Keyword(s):  
Escherichia Coli ◽  
Salmonella Enterica ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Cross Linking ◽  
Atp Binding ◽  
Cross Link ◽  
Atp Binding Cassette Transporter ◽  
Serovar Typhimurium ◽  
Atp Binding Cassette

ABSTRACT We have investigated the interaction of the uncommonly large periplasmic P2 loop of the MalF subunit of the maltose ATP-binding cassette transporter (MalFGK2) from Escherichia coli and Salmonella enterica serovar Typhimurium with maltose binding protein (MalE) by site-specific chemical cross-linking in the assembled transport complex. We focused on possible distance changes between two pairs of residues of the P2 loop and MalE during the transport cycle. The distance between MalF(S205C) and MalE(T80C) (∼5 Å) remained unchanged under all conditions tested. Cross-linking did not affect the ATPase activity of the complex. The distance between MalF(T177C) and MalE(T31C) changed from ∼10 Å to ∼5 Å upon binding of ATP (or maltose, with a less pronounced result) and was reset to ∼10 Å after hydrolysis of one ATP. A cross-link (∼25 Å) between MalF(S205C) and MalE(T31C) was observed only when the transporter resided in a transition state-like conformation, as was the case after vanadate trapping or in a binding protein-independent mutant, both of which are characterized by tight binding of unliganded MalE to the transporter. Thus, we propose that the observed cross-link is indicative of catalytic intermediates of the transporter. Together, our results strengthen the notion that the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. The data are discussed with respect to a crystal structure and current transport models.

scholarly journals Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2

2017 ◽  
Vol 19 (14) ◽  
pp. 9366-9373 ◽  
Author(s):  
Jingwei Weng ◽  
Shuo Gu ◽  
Xin Gao ◽  
Xuhui Huang ◽  
Wenning Wang
Keyword(s):  
Abc Transporter ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Atp Binding ◽  
Type I ◽  
Closed Conformation ◽  
Atp Binding Cassette Transporter ◽  
Maltose Transporter ◽  
Atp Binding Cassette

Maltose transporter MalFGK2is a type-I importer in the ATP-binding cassette (ABC) transporter superfamily.

Periplasmic Loop P2 of the MalF Subunit of the Maltose ATP Binding Cassette Transporter Is Sufficient To Bind the Maltose Binding Protein MalE†

Biochemistry ◽  
2009 ◽  
Vol 48 (10) ◽  
pp. 2216-2225 ◽  
Author(s):  
Tomas Jacso ◽  
Mathias Grote ◽  
Martin L. Daus ◽  
Peter Schmieder ◽  
Sandro Keller ◽  
...  
Keyword(s):  
Binding Protein ◽  
Maltose Binding Protein ◽  
Atp Binding ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

In silico characterization of TTHA0596: A potential Zn 2+ binding protein of ATP-binding cassette transporter

Gene Reports ◽  
2017 ◽  
Vol 6 ◽  
pp. 132-141 ◽  
Author(s):  
Suraj Kumar Mandal ◽  
Monika Chandravanshi ◽  
Prerana Gogoi ◽  
Shankar Prasad Kanaujia
Keyword(s):  
In Silico ◽  
Binding Protein ◽  
Atp Binding ◽  
Atp Binding Cassette Transporter ◽  
In Silico Characterization ◽  
Atp Binding Cassette
Sign in / Sign up

Export Citation Format

Share Document