3r3p: Difference between revisions
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[[ | ==Homing Endonuclease I-Bth0305I Catalytic Domain== | ||
<StructureSection load='3r3p' size='340' side='right' caption='[[3r3p]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3r3p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Viruses Viruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R3P FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF029, 0305phi8-36p029 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10239 Viruses])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r3p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r3p RCSB], [http://www.ebi.ac.uk/pdbsum/3r3p PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Novel family of putative homing endonuclease genes was recently discovered during analyses of metagenomic and genomic sequence data. One such protein is encoded within a group I intron that resides in the recA gene of the Bacillus thuringiensis 03058-36 bacteriophage. Named I-Bth0305I, the endonuclease cleaves a DNA target in the uninterrupted recA gene at a position immediately adjacent to the intron insertion site. The enzyme displays a multidomain, homodimeric architecture and footprints a DNA region of approximately 60 bp. Its highest specificity corresponds to a 14-bp pseudopalindromic sequence that is directly centered across the DNA cleavage site. Unlike many homing endonucleases, the specificity profile of the enzyme is evenly distributed across much of its target site, such that few single base pair substitutions cause a significant decrease in cleavage activity. A crystal structure of its C-terminal domain confirms a nuclease fold that is homologous to very short patch repair (Vsr) endonucleases. The domain architecture and DNA recognition profile displayed by I-Bth0305I, which is the prototype of a homing lineage that we term the 'EDxHD' family, are distinct from previously characterized homing endonucleases. | |||
Activity, specificity and structure of I-Bth0305I: a representative of a new homing endonuclease family.,Taylor GK, Heiter DF, Pietrokovski S, Stoddard BL Nucleic Acids Res. 2011 Sep 2. PMID:21890897<ref>PMID:21890897</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | |||
== | |||
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[[Category: Viruses]] | [[Category: Viruses]] | ||
[[Category: Stoddard, B L.]] | [[Category: Stoddard, B L.]] | ||
Revision as of 07:46, 5 June 2014
Homing Endonuclease I-Bth0305I Catalytic DomainHoming Endonuclease I-Bth0305I Catalytic Domain
Structural highlights
Publication Abstract from PubMedNovel family of putative homing endonuclease genes was recently discovered during analyses of metagenomic and genomic sequence data. One such protein is encoded within a group I intron that resides in the recA gene of the Bacillus thuringiensis 03058-36 bacteriophage. Named I-Bth0305I, the endonuclease cleaves a DNA target in the uninterrupted recA gene at a position immediately adjacent to the intron insertion site. The enzyme displays a multidomain, homodimeric architecture and footprints a DNA region of approximately 60 bp. Its highest specificity corresponds to a 14-bp pseudopalindromic sequence that is directly centered across the DNA cleavage site. Unlike many homing endonucleases, the specificity profile of the enzyme is evenly distributed across much of its target site, such that few single base pair substitutions cause a significant decrease in cleavage activity. A crystal structure of its C-terminal domain confirms a nuclease fold that is homologous to very short patch repair (Vsr) endonucleases. The domain architecture and DNA recognition profile displayed by I-Bth0305I, which is the prototype of a homing lineage that we term the 'EDxHD' family, are distinct from previously characterized homing endonucleases. Activity, specificity and structure of I-Bth0305I: a representative of a new homing endonuclease family.,Taylor GK, Heiter DF, Pietrokovski S, Stoddard BL Nucleic Acids Res. 2011 Sep 2. PMID:21890897[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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