Literature DB >> 12869697

Long-distance conformational changes in a protein engineered by modulated sequence duplication.

Martin Sagermann1, Leslie Gay, Brian W Matthews.   

Abstract

There are few, if any, known instances in which a biological signal is transmitted via a large conformational change through the body of a protein. We describe here a mutant of T4 lysozyme that was engineered to permit structural change at a distance. The design uses a tandem sequence repeat that makes it possible to transmit large-scale structural changes from one end of an alpha-helix to the other over a distance of 17-25 A. The method should be of general applicability and may make it possible to introduce a mutation at one site in a protein that will induce large-scale changes in the structure at a spatially remote site.

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Year:  2003        PMID： 12869697      PMCID： PMC170894          DOI： 10.1073/pnas.1633549100

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  23 in total

1.  A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis.

Authors:  Xue-jun Zhang; Walter A Baase; Brian W Matthews
Journal:  Biophys Chem       Date:  2002-12-10       Impact factor: 2.352

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Authors:  B W Matthews
Journal:  Biochemistry       Date:  1987-11-03       Impact factor: 3.162

4.  Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.

Authors:  H Nicholson; W J Becktel; B W Matthews
Journal:  Nature       Date:  1988-12-15       Impact factor: 49.962

Review 5.  3D domain swapping: a mechanism for oligomer assembly.

Authors:  M J Bennett; M P Schlunegger; D Eisenberg
Journal:  Protein Sci       Date:  1995-12       Impact factor: 6.725

Review 6.  Regulation of signal transduction and signal diversity by receptor oligomerization.

Authors:  M A Lemmon; J Schlessinger
Journal:  Trends Biochem Sci       Date:  1994-11       Impact factor: 13.807

Review 7.  An analysis of packing in the protein folding problem.

Authors:  F M Richards; W A Lim
Journal:  Q Rev Biophys       Date:  1993-11       Impact factor: 5.318

8.  Human growth hormone and extracellular domain of its receptor: crystal structure of the complex.

Authors:  A M de Vos; M Ultsch; A A Kossiakoff
Journal:  Science       Date:  1992-01-17       Impact factor: 47.728

9.  Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis.

Authors:  D W Heinz; W A Baase; X J Zhang; M Blaber; F W Dahlquist; B W Matthews
Journal:  J Mol Biol       Date:  1994-02-25       Impact factor: 5.469

10.  Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.

Authors:  M Sagermann; W A Baase; B W Matthews
Journal:  Proc Natl Acad Sci U S A       Date:  1999-05-25       Impact factor: 11.205
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  6 in total

1.  Sequential reorganization of beta-sheet topology by insertion of a single strand.

Authors:  Martin Sagermann; Walter A Baase; Brian W Matthews
Journal:  Protein Sci       Date:  2006-04-05       Impact factor: 6.725

2.  Beta-strand flipping and slipping triggered by turn replacement reveal the opportunistic nature of beta-strand pairing.

Authors:  Koki Makabe; Shude Yan; Valentina Tereshko; Grzegorz Gawlak; Shohei Koide
Journal:  J Am Chem Soc       Date:  2007-11-07       Impact factor: 15.419

3.  Molecular dynamics simulations of an engineered T4 lysozyme exclude helix to sheet transition, and provide insights into long distance, intra-protein switchable motion.

Authors:  Laurence Biggers; Hadeer Elhabashy; Edward Ackad; Mohammad S Yousef
Journal:  Protein Sci       Date:  2019-11-21       Impact factor: 6.725

4.  Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme.

Authors:  Mohammad S Yousef; Nicole Bischoff; Collin M Dyer; Walter A Baase; Brian W Matthews
Journal:  Protein Sci       Date:  2006-04       Impact factor: 6.725

5.  Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme.

Authors:  Mohammad S Yousef; Walter A Baase; Brian W Matthews
Journal:  Proc Natl Acad Sci U S A       Date:  2004-07-30       Impact factor: 11.205

6.  A 200 nanoseconds all-atom simulation of the pH-dependent EF loop transition in bovine β-lactoglobulin. The role of the orientation of the E89 side chain.

Authors:  Kiara Fenner; Arthur Redgate; Lorenzo Brancaleon
Journal:  J Biomol Struct Dyn       Date:  2020-09-10
  6 in total

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