ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2). (Q38301178)

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scientific article published on June 2007

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English	ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2).	scientific article published on June 2007

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scholarly article

1 reference

Europe PubMed Central

1 September 2017

ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2). (English)

1 reference

Europe PubMed Central

1 September 2017

author name string

Martin L Daus

1

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Europe PubMed Central

1 September 2017

Mathias Grote

2

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Europe PubMed Central

1 September 2017

Peter Müller

3

1 reference

Europe PubMed Central

1 September 2017

Meike Doebber

4

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Europe PubMed Central

1 September 2017

Andreas Herrmann

5

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Europe PubMed Central

1 September 2017

Heinz-Jürgen Steinhoff

6

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Europe PubMed Central

1 September 2017

Elie Dassa

7

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Europe PubMed Central

1 September 2017

Erwin Schneider

8

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Europe PubMed Central

1 September 2017

language of work or name

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publication date

1 June 2007

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Europe PubMed Central

1 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

1 September 2017

282

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Europe PubMed Central

1 September 2017

22387-22396

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Europe PubMed Central

1 September 2017

31

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Europe PubMed Central

1 September 2017

The ABC transporter structure and mechanism: perspectives on recent research.

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The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence

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ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation

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ATP induces conformational changes of periplasmic loop regions of the maltose ATP-binding cassette transporter

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Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport

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A Cys-less variant of the bacterial ATP binding cassette protein MalK is functional in maltose transport and regulation

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Large-scale purification, dissociation and functional reassembly of the maltose ATP-binding cassette transporter (MalFGK(2)) of Salmonella typhimurium

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Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis

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Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters

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Functional consequences of mutations in the conserved 'signature sequence' of the ATP-binding-cassette protein MalK.

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Mutational analysis of conserved carboxylate residues in the nucleotide binding sites of P-glycoprotein

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A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer

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Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly

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Nucleotide-induced conformational changes in P-glycoprotein and in nucleotide binding site mutants monitored by trypsin sensitivity.

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The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporter

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The role of the conserved glycines of ATP-binding cassette signature motifs of MRP1 in the communication between the substrate-binding site and the catalytic centers.

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Simulation of the coupling between nucleotide binding and transmembrane domains in the ATP binding cassette transporter BtuCD.

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The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA.

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Identifiers

10.1074/JBC.M701979200

1 reference

Europe PubMed Central

1 September 2017

1 reference

Europe PubMed Central

1 September 2017

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