Literature DB >> 8513890

Location of tolerated insertions/deletions in the structure of the maltose binding protein.

J M Betton1, P Martineau, W Saurin, M Hofnung.   

Abstract

In a previous study [(1987) J. Mol. Biol. 194, 663-673], we isolated ten insertion/deletion mutants (indels) of the maltose binding protein for which the maltose binding constant was only a little or not at all affected. In this paper, we have localized these mutations in the recently solved three-dimensional structure. Contrary to the general expectation, most of the insertion/deletion modifications occurred within elements of secondary structure. An analysis of the inserted residues for three indels found within alpha helices allowed an interpretation regarding protein structure accommodation to such modifications.

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Year:  1993        PMID: 8513890     DOI: 10.1016/0014-5793(93)81409-s

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins.

Authors:  Karen M Routzahn; David S Waugh
Journal:  J Struct Funct Genomics       Date:  2002

2.  In vivo assembly of active maltose binding protein from independently exported protein fragments.

Authors:  J M Betton; M Hofnung
Journal:  EMBO J       Date:  1994-03-01       Impact factor: 11.598

3.  Permissible peptide insertions surrounding the signal peptide-mature protein junction of the ClpG prepilin: CS31A fimbriae of Escherichia coli as carriers of foreign sequences.

Authors:  M Der Vartanian; M C Méchin; B Jaffeux; Y Bertin; I Félix; B Gaillard-Martinie
Journal:  Gene       Date:  1994-10-11       Impact factor: 3.688

  3 in total

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