Type II restriction endonuclease R.Hpy188I belongs to the GIY-YIG nuclease superfamily, but exhibits an unusual active site

January 2008
BMC Structural Biology;2008, Vol. 8, p48
Academic Journal
No abstract available.


Related Articles

  • Tetrameric restriction enzymes: expansion to the GIY-YIG nuclease family. Gasiunas, Giedrius; Sasnauskas, Giedrius; Tamulaitis, Gintautas; Urbanke, Claus; Razaniene, Dalia; Siksnys, Virginijus // Nucleic Acids Research;2007, Vol. 36 Issue 3, p938 

    The GIY-YIG nuclease domain was originally identified in homing endonucleases and enzymes involved in DNA repair and recombination. Many of the GIY-YIG family enzymes are functional as monomers. We show here that the Cfr42I restriction endonuclease which belongs to the GIY-YIG family and...

  • Crystallographic and Bioinformatic Studies on Restriction Endonucleases: Inference of Evolutionary Relationships in the “Midnight Zone” of Homology. Bujnicki, Janusz M. // Current Protein & Peptide Science;Oct2003, Vol. 4 Issue 5, p327 

    Type II restriction endonucleases (ENases) cleave DNA with remarkable sequence specificity. Their discovery in 1970 and studies on molecular genetics and biochemistry carried out over the past four decades laid foundations for recombinant DNA techniques. Today, restriction enzymes are...

  • I-Ssp6803I: the first homing endonuclease from the PD-(D/E)XK superfamily exhibits an unusual mode of DNA recognition. Janusz M. Bujnicki // Bioinformatics;Mar2007, Vol. 23 Issue 5, p527 

    Motivation: Restriction endonucleases (REases) and homing endonucleases (HEases) are biotechnologically important enzymes. Nearly all structurally characterized REases belong to the PD-(D/E)XK superfamily of nucleases, while most HEases belong to an unrelated LAGLIDADG superfamily. These two...

  • The monomeric GIY-YIG homing endonuclease I-BmoI uses a molecular anchor and a flexible tether to sequentially nick DNA. Kleinstiver, Benjamin P.; Wolfs, Jason M.; Edgell, David R. // Nucleic Acids Research;May2013, Vol. 41 Issue 10, p5413 

    The GIY-YIG nuclease domain is found within protein scaffolds that participate in diverse cellular pathways and contains a single active site that hydrolyzes DNA by a one-metal ion mechanism. GIY-YIG homing endonucleases (GIY-HEs) are two-domain proteins with N-terminal GIY-YIG nuclease domains...

  • Crystal structure of the Holliday junction resolving enzyme T7 endonuclease I. Hadden, Jonathan M.; Convery, Máire A.; Déclais, Anne-Cécile; Lilley, David M.J.; Phillips, Simon E.V. // Nature Structural Biology;Jan2001, Vol. 8 Issue 1, p62 

    We have solved the crystal structure of the Holliday junction resolving enzyme T7 endonuclease I at 2.1 Ã… resolution using the multiwavelength anomalous dispersion (MAD) technique. Endonuclease I exhibits strong structural specificity for four-way DNA junctions. The structure shows that it...

  • WebFARM: web server for finite automated restriction mapping. Singh, Tiratha Raj // Bioinformation;2010, Vol. 4 Issue 8, p341 

    Restriction endonucleases are indispensable tools in molecular biology and biotechnology. Type II restriction endonucleases are part of restriction modification systems. DNA fragment extraction and restriction mapping are the basis for several biotechnological activities. WebFARM is a server...

  • A homology model of restriction endonuclease SfiI in complex with DNA. Chmiel, Agnieszka A.; Bujnicki, Janusz M.; Skowronek, Krzysztof J. // BMC Structural Biology;2005, Vol. 5, p2 

    Background: Restriction enzymes (REases) are commercial reagents commonly used in recombinant DNA technologies. They are attractive models for studying protein-DNA interactions and valuable targets for protein engineering. They are, however, extremely divergent: the amino acid sequence of a...

  • Metal ions bound at the active site of the junction-resolving enzyme T7 endonuclease I. Hadden, Jonathan M.; Déclais, Anne-Cécile; Phillips, Simon E.V.; Lilley, David M.J. // EMBO Journal;7/1/2002, Vol. 21 Issue 13, p3505 

    T7 endonuclease I is a nuclease that is selective for the structure of the four-way DNA junction. The active site is similar to those of a number of restriction enzymes. We have solved the crystal structure of endonuclease I with a wild-type active s

  • Phylogenomic analysis of the GIY-YIG nuclease superfamily. Dunin-Horkawicz, Stanislaw; Feder, Marcin; Bujnicki, Janusz M // BMC Genomics;2006, Vol. 7, p98 

    Background: The GIY-YIG domain was initially identified in homing endonucleases and later in other selfish mobile genetic elements (including restriction enzymes and non-LTR retrotransposons) and in enzymes involved in DNA repair and recombination. However, to date no systematic search for novel...

  • Structural and evolutionary classification of Type II restriction enzymes based on theoretical and experimental analyses. Orlowski, Jerzy; Bujnicki, Janusz M. // Nucleic Acids Research;2008, Vol. 36 Issue 11, p3552 

    For a very long time, Type II restriction enzymes (REases) have been a paradigm of ORFans: proteins with no detectable similarity to each other and to any other protein in the database, despite common cellular and biochemical function. Crystallographic analyses published until January 2008...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics