Malctose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport

Journal of Biological Chemistry

Volumn 279, Issue 27, 2004, Pages 28243-28250

  Austermuhle, Mariana I ^a   Hall, Jason A ^b   Klug, Candice S ^c   Davidson, Amy L ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b University of Texas Medical Branch School of Medicine   (United States)

^c MEDICAL COLLEGE OF WISCONSIN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BIOCHEMISTRY; CATALYSTS; COMPLEXATION; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; HYDROLYSIS; MALTOSE;

CATALYTIC TRANSITIONS; MALTOSE-BINDING PROTEINS (MBP); MEMBRANE-ASSOCIATED TRANSPORTER;

PROTEINS;

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; BACTERIAL PROTEIN; CYSTEINE; MALF PROTEIN; MALFGK2 PROTEIN; MALG PROTEIN; MALK PROTEIN; MALTOSE; MALTOSE BINDING PROTEIN; UNCLASSIFIED DRUG; VANADIC ACID; CARRIER PROTEIN; LIGAND; MALTOSE-BINDING PROTEIN;

ARTICLE; C TERMINAL DOMAIN; CATALYSIS; CONFORMATIONAL TRANSITION; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN IMMOBILIZATION; PROTEIN INTERACTION; SPIN LABELING; SUGAR TRANSPORT; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; CHROMATOGRAPHY; CYTOPLASM; METABOLISM; MOLECULAR CLONING; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; TRANSPORT AT THE CELLULAR LEVEL; X RAY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATE; BIOLOGICAL TRANSPORT; CARRIER PROTEINS; CATALYSIS; CHROMATOGRAPHY; CLONING, MOLECULAR; CYSTEINE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; HYDROLYSIS; LIGANDS; MALTOSE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PERIPLASM; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SPIN LABELS; VANADATES; X-RAYS;

EID: 3142619074     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M403508200     Document Type: Article

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