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SecB-A chaperone dedicated to protein translocation

Bechtluft, P., Nouwen, N., Tans, S. J. & Driessen, A. J. M., 2010, In : Molecular BioSystems. 6, 4, p. 620-627 8 p.

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  • SecB—A chaperone dedicated to protein translocation

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DOI

SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.

Original languageEnglish
Pages (from-to)620-627
Number of pages8
JournalMolecular BioSystems
Volume6
Issue number4
Publication statusPublished - 2010

    Keywords

  • MALTOSE-BINDING PROTEIN, BACTERIAL CYTOPLASMIC MEMBRANE, ESCHERICHIA-COLI, SIGNAL SEQUENCE, ANTIFOLDING ACTIVITY, DENATURED PROTEINS, SUBSTRATE PROTEIN, CRYSTAL-STRUCTURE, FOLDING PATHWAY, TRIGGER FACTOR

ID: 2562291