scholarly journals Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter

2015 ◽  
Vol 98 (5) ◽  
pp. 878-894 ◽  
Author(s):  
Frances Joan D. Alvarez ◽  
Cédric Orelle ◽  
Yan Huang ◽  
Ruchika Bajaj ◽  
R. Michael Everly ◽  
...  
Keyword(s):  
Binding Protein ◽  
Maltose Binding Protein ◽  
Atp Binding ◽  
Maltose Transporter ◽  
Atp Binding Cassette

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.

scholarly journals Exploring the Role of Integral Membrane Proteins in ATP-Binding Cassette Transporters: Analysis of a Collection of MalG Insertion Mutants

1998 ◽  
Vol 180 (9) ◽  
pp. 2507-2514 ◽  
Author(s):  
Bryn D. Nelson ◽  
Beth Traxler
Keyword(s):  
Membrane Proteins ◽  
Cytoplasmic Membrane ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Integral Membrane Proteins ◽  
Atp Binding ◽  
Mutant Proteins ◽  
Transport Complex ◽  
Atp Binding Cassette

ABSTRACT The maltose transport complex of Escherichia coli is a well-studied example of an ATP-binding cassette transporter. The complex, containing one copy each of the integral membrane proteins MalG and MalF and two copies of the peripheral cytoplasmic membrane protein MalK, interacts with the periplasmic maltose-binding protein to efficiently translocate maltose and maltodextrins across the bacterial cytoplasmic membrane. To investigate the role of MalG both in MalFGK2 assembly interactions and in subsequent transport interactions, we isolated and characterized 18 different MalG mutants, each containing a 31-residue insertion in the protein. Eight insertions mapping to distinct hydrophilic regions of MalG permitted either assembly or both assembly and transport interactions to occur. In particular, we isolated two insertions mapping to extracytoplasmic (periplasmic) regions of MalG which preserved both assembly and transport abilities, suggesting that these are permissive sites in the protein. Another periplasmic insertion seems to affect only transport-specific interactions between MalG and maltose-binding protein, defining a novel class of MalG mutants. Finally, four MalG mutant proteins, although stably expressed, are unable to assemble into the MalFGK2 complex. These mutants contain insertions in only two different hydrophilic regions of MalG, consistent with the notion that a restricted number of domains in this protein are critical complex assembly determinants. These MalG mutants will allow us to further explore the intermolecular interactions of this model transporter.

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 Biochemical evidence for the presence of two α-glucoside ABC-transport systems in the hyperthermophilic archaeonPyrococcus furiosus

Archaea ◽  
2002 ◽  
Vol 1 (1) ◽  
pp. 19-25 ◽  
Author(s):  
Sonja M. Koning ◽  
Wil N. Konings ◽  
Arnold J.M. Driessen
Keyword(s):  
Transport System ◽  
Pyrococcus Furiosus ◽  
Binding Protein ◽  
Transport Systems ◽  
Atp Binding ◽  
Hyperthermophilic Archaeon ◽  
Biochemical Evidence ◽  
Abc Transport ◽  
Maltose Transporter ◽  
Atp Binding Cassette

The hyperthermophilic archaeonPyrococcus furiosuscan utilize different carbohydrates, such as starch, maltose and trehalose. Uptake of α-glucosides is mediated by two different, binding protein-dependent, ATP-binding cassette (ABC)-type transport systems. The maltose transporter also transports trehalose, whereas the maltodextrin transport system mediates the uptake of maltotriose and higher malto-oligosaccharides, but not maltose. Both transport systems are induced during growth on their respective substrates.

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

scholarly journals Identification and Characterization of an ATP Binding Cassette l-Carnitine Transporter inListeria monocytogenes

2000 ◽  
Vol 66 (11) ◽  
pp. 4696-4704 ◽  
Author(s):  
Katy R. Fraser ◽  
Duncan Harvie ◽  
Peter J. Coote ◽  
Conor P. O'Byrne
Keyword(s):  
Binding Protein ◽  
Substrate Binding ◽  
Compatible Solutes ◽  
Brain Heart Infusion ◽  
Defined Medium ◽  
Compatible Solute ◽  
Atp Binding ◽  
Insertional Inactivation ◽  
Substrate Binding Protein ◽  
Atp Binding Cassette

ABSTRACT We identified an operon in Listeria monocytogenes EGD with high levels of sequence similarity to the operons encoding the OpuC and OpuB compatible solute transporters from Bacillus subtilis, which are members of the ATP binding cassette (ABC) substrate binding protein-dependent transporter superfamily. The operon, designated opuC, consists of four genes which are predicted to encode an ATP binding protein (OpuCA), an extracellular substrate binding protein (OpuCC), and two membrane-associated proteins presumed to form the permease (OpuCB and OpuCD). The operon is preceded by a potential SigB-dependent promoter. An opuC-defective mutant was generated by the insertional inactivation of theopuCA gene. The mutant was impaired for growth at high osmolarity in brain heart infusion broth and failed to grow in a defined medium. Supplementation of the defined medium with peptone restored the growth of the mutant in this medium. The mutant was found to accumulate the compatible solutes glycine betaine and choline to same extent as the parent strain but was defective in the uptake ofl-carnitine. We conclude that the opuC operon in L. monocytogenes encodes an ABC compatible solute transporter which is capable of transporting l-carnitine and which plays an important role in osmoregulation in this pathogen.

scholarly journals Maltose/Maltodextrin System of Escherichia coli: Transport, Metabolism, and Regulation

1998 ◽  
Vol 62 (1) ◽  
pp. 204-229 ◽  
Author(s):  
Winfried Boos ◽  
Howard Shuman
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Transcriptional Control ◽  
Sugar Transport ◽  
Receptor Protein ◽  
Dimensional Structure ◽  
Atp Binding ◽  
Functional Sites ◽  
Maltose Transporter ◽  
Atp Binding Cassette

SUMMARY The maltose system of Escherichia coli offers an unusually rich set of enzymes, transporters, and regulators as objects of study. This system is responsible for the uptake and metabolism of glucose polymers (maltodextrins), which must be a preferred class of nutrients for E. coli in both mammalian hosts and in the environment. Because the metabolism of glucose polymers must be coordinated with both the anabolic and catabolic uses of glucose and glycogen, an intricate set of regulatory mechanisms controls the expression of mal genes, the activity of the maltose transporter, and the activities of the maltose/maltodextrin catabolic enzymes. The ease of isolating many of the mal gene products has contributed greatly to the understanding of the structures and functions of several classes of proteins. Not only was the outer membrane maltoporin, LamB, or the phage lambda receptor, the first virus receptor to be isolated, but also its three-dimensional structure, together with extensive knowledge of functional sites for ligand binding as well as for phage λ binding, has led to a relatively complete description of this sugar-specific aqueous channel. The periplasmic maltose binding protein (MBP) has been studied with respect to its role in both maltose transport and maltose taxis. Again, the combination of structural and functional information has led to a significant understanding of how this soluble receptor participates in signaling the presence of sugar to the chemosensory apparatus as well as how it participates in sugar transport. The maltose transporter belongs to the ATP binding cassette family, and although its structure is not yet known at atomic resolution, there is some insight into the structures of several functional sites, including those that are involved in interactions with MBP and recognition of substrates and ATP. A particularly astonishing discovery is the direct participation of the transporter in transcriptional control of the mal regulon. The MalT protein activates transcription at all mal promoters. A subset also requires the cyclic AMP receptor protein for transcription. The MalT protein requires maltotriose and ATP as ligands for binding to a dodecanucleotide MalT box that appears in multiple copies upstream of all mal promoters. Recent data indicate that the ATP binding cassette transporter subunit MalK can directly inhibit MalT when the transporter is inactive due to the absence of substrate. Despite this wealth of knowledge, there are still basic issues that require clarification concerning the mechanism of MalT-mediated activation, repression by the transporter, biosynthesis and assembly of the outer membrane and inner membrane transporter proteins, and interrelationships between the mal enzymes and those of glucose and glycogen metabolism.

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