Arg149 is involved in switching the low affinity, open state of the binding protein AfProX into its high affinity, closed state

Journal of Molecular Biology

Volumn 411, Issue 1, 2011, Pages 36-52

  Tschapek, Britta ^a   Pittelkow, Marco ^b   Sohn Bösser, Linda ^b   Holtmann, Gudrun ^b   Smits, Sander H J ^a   Gohlke, Holger ^a   Bremer, Erhard ^b   Schmitt, Lutz ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

ABC transporter; glycine betaine; ligand binding site; substrate binding protein; substrate recognition

Indexed keywords

ABC TRANSPORTER; ARGININE; BACTERIAL PROTEIN; BETAINE; BINDING PROTEIN; PROLINE; PROTEIN PRO X; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARCHAEOGLOBUS FULGIDUS; ARTICLE; BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; GENE SWITCHING; HYPERTHERMOPHILIC ARCHAEON; LIGAND BINDING; MOLECULAR DYNAMICS; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

ARCHAEA; ARCHAEOGLOBUS FULGIDUS;

EID: 79960697231     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.05.039     Document Type: Article

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