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)

Journal of Biological Chemistry

Volumn 282, Issue 31, 2007, Pages 22387-22396

  Daus, Martin L ^a   Grote, Mathias ^a   Müller, Peter ^a   Doebber, Meike ^b   Herrmann, Andreas ^a   Steinhoff, Heinz Jürgen ^b   Dassa, Elie ^c   Schneider, Erwin ^a  

^a HUMBOLDT UNIVERSITY   (Germany)

^b UNIVERSITY OF OSNABRÜCK   (Germany)

^c INSTITUT PASTEUR   (France)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; CROSSLINKING; MALTOSE; MONOMERS;

CYSTEINES; MALTOSE TRANSPORTERS; TRANSLOCATION CYCLES;

DIMERS;

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; CROSS LINKING; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN MOTIF; STRUCTURE ANALYSIS;

ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ATP-BINDING CASSETTE TRANSPORTERS; BIOLOGICAL TRANSPORT; CROSS-LINKING REAGENTS; DIMERIZATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MALTOSE; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MONOSACCHARIDE TRANSPORT PROTEINS; PROTEOLIPIDS;

EID: 34547936010     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M701979200     Document Type: Article

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