Periplasmic binding proteins: a versatile superfamily for protein engineering
- PMID: 15313245
- DOI: 10.1016/j.sbi.2004.07.004
Periplasmic binding proteins: a versatile superfamily for protein engineering
Abstract
The diversity of biological function, ligand binding, conformational changes and structural adaptability of the periplasmic binding protein superfamily have been exploited to engineer biosensors, allosteric control elements, biologically active receptors and enzymes using a combination of techniques, including computational design. Extensively redesigned periplasmic binding proteins have been re-introduced into bacteria to function in synthetic signal transduction pathways that respond to extracellular ligands and as biologically active enzymes.
Similar articles
-
Computational design of receptor and sensor proteins with novel functions.Nature. 2003 May 8;423(6936):185-90. doi: 10.1038/nature01556. Nature. 2003. PMID: 12736688
-
Computational design of a biologically active enzyme.Science. 2004 Jun 25;304(5679):1967-71. doi: 10.1126/science.1098432. Science. 2004. PMID: 15218149 Retracted.
-
Computational biology: Biosensor design.Nature. 2003 May 8;423(6936):132-3. doi: 10.1038/423132a. Nature. 2003. PMID: 12736670 No abstract available.
-
Maltose-binding protein: a versatile platform for prototyping biosensing.Curr Opin Biotechnol. 2006 Feb;17(1):17-27. doi: 10.1016/j.copbio.2006.01.002. Epub 2006 Jan 18. Curr Opin Biotechnol. 2006. PMID: 16413768 Review.
-
Engineering allosteric regulation into biological catalysts.Chembiochem. 2009 Dec 14;10(18):2824-35. doi: 10.1002/cbic.200900590. Chembiochem. 2009. PMID: 19937897 Review.
Cited by
-
Searching for EGF Fragments Recreating the Outer Sphere of the Growth Factor Involved in Receptor Interactions.Int J Mol Sci. 2024 Jan 25;25(3):1470. doi: 10.3390/ijms25031470. Int J Mol Sci. 2024. PMID: 38338748 Free PMC article.
-
Revealing Allosteric Mechanism of Amino Acid Binding Proteins from Open to Closed State.Molecules. 2023 Oct 17;28(20):7139. doi: 10.3390/molecules28207139. Molecules. 2023. PMID: 37894619 Free PMC article.
-
Retracing the evolution of a modern periplasmic binding protein.Protein Sci. 2023 Nov;32(11):e4793. doi: 10.1002/pro.4793. Protein Sci. 2023. PMID: 37788980 Free PMC article.
-
Conformational Changes in Surface-Immobilized Proteins Measured Using Combined Atomic Force and Fluorescence Microscopy.Molecules. 2023 Jun 8;28(12):4632. doi: 10.3390/molecules28124632. Molecules. 2023. PMID: 37375186 Free PMC article.
-
Emergence of an Auxin Sensing Domain in Plant-Associated Bacteria.mBio. 2023 Feb 28;14(1):e0336322. doi: 10.1128/mbio.03363-22. Epub 2023 Jan 5. mBio. 2023. PMID: 36602305 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources