PMID: 9187655Jun 1, 1997Paper

The structure of I-Crel, a group I intron-encoded homing endonuclease

Nature Structural Biology
P J HeathB L Stoddard

Abstract

The structure of I-Crel provides the first view of a protein encoded by a gene within an intron. This endonuclease recognizes a long DNA site approximately 20 base pairs in length and facilitates the lateral transfer of that intron. The protein exhibits a DNA-binding surface consisting of four antiparallel beta-strands that form a 20 A wide groove which is over 70 A long. The architecture of this fold is different from that of the TATA binding protein, TBP, which also contains an antiparallel beta-saddle. The conserved LAGLIDADG motif, which is found in many mobile intron endonucleases, maturases and inteins, forms a novel helical interface and contributes essential residues to the active site.

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Citations

Jan 7, 1998·Protein Science : a Publication of the Protein Society·K E FlickB L Stoddard
May 22, 2003·Journal of Molecular Biology·Brett ChevalierBarry L Stoddard
Apr 8, 2000·FEMS Microbiology Letters·F S Gimble
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Nov 7, 2002·Molecular Cell·Brett S ChevalierBarry L Stoddard
Jun 1, 1997·Nature Structural Biology·A K Aggarwal
Jul 1, 1997·Nature Structural Biology
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Feb 13, 2001·Nucleic Acids Research·P LucasC Lemieux
Aug 31, 2002·Nucleic Acids Research·Lenny M SeligmanAdeline L Veillet
May 29, 2003·Nucleic Acids Research·Jean-Charles EpinatEmmanuel Lacroix
Jun 11, 2004·Nucleic Acids Research·George H Silva, Marlene Belfort
Jul 29, 2004·Nucleic Acids Research·Karen L PoseyFrederick S Gimble
Feb 4, 2006·Nucleic Acids Research·James C SamuelsonShuang-yong Xu
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Apr 9, 2017·Applied Microbiology and Biotechnology·Ashraf S A El-SayedGul Shad Ali

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