scholarly journals Active transport of maltose in Escherichia coli K12. Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane.

1982 ◽  
Vol 257 (10) ◽  
pp. 5455-5461
Author(s):  
H A Shuman
Keyword(s):  
Escherichia Coli ◽  
Active Transport ◽  
Cytoplasmic Membrane ◽  
Binding Protein ◽  
Substrate Recognition ◽  
Maltose Binding Protein ◽  
Recognition Site ◽  
Escherichia Coli K12

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.

Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12

1987 ◽  
Vol 194 (4) ◽  
pp. 663-673 ◽  
Author(s):  
Pascale Duplay ◽  
Sevec Szmelcman ◽  
Hugues Bedouelle ◽  
Maurice Hofnung
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Functional Changes ◽  
Escherichia Coli K12

scholarly journals Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12.

1984 ◽  
Vol 259 (16) ◽  
pp. 10606-10613 ◽  
Author(s):  
P Duplay ◽  
H Bedouelle ◽  
A Fowler ◽  
I Zabin ◽  
W Saurin ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Escherichia Coli K12 ◽  
Male Gene
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