1t2t
From Proteopedia
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- | [[Image:1t2t.gif|left|200px]] | ||
- | + | ==Crystal structure of the DNA-binding domain of intron endonuclease I-TevI with operator site== | |
- | + | <StructureSection load='1t2t' size='340' side='right'caption='[[1t2t]], [[Resolution|resolution]] 2.50Å' scene=''> | |
- | + | == Structural highlights == | |
- | | | + | <table><tr><td colspan='2'>[[1t2t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T2T FirstGlance]. <br> |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2t OCA], [https://pdbe.org/1t2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t2t RCSB], [https://www.ebi.ac.uk/pdbsum/1t2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t2t ProSAT]</span></td></tr> | |
- | + | </table> | |
- | + | == Function == | |
- | + | [https://www.uniprot.org/uniprot/TEV1_BPT4 TEV1_BPT4] This endonuclease is specific to the thymidylate synthase (td) gene splice junction and is involved in intron homing. | |
- | + | == Evolutionary Conservation == | |
- | == | + | [[Image:Consurf_key_small.gif|200px|right]] |
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t2/1t2t_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t2t ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
Customary binding sites of intron-encoded homing endonucleases lie within cognate intronless alleles, at the so-called homing sites. Here, we describe a novel, high-affinity binding site for I-TevI endonuclease, encoded within the group I td intron of phage T4. This site is an operator that overlaps the T4 late promoter, which drives I-TevI expression from within the td intron. I-TevI binds the operator and homing sites with equal affinity, and functions as a transcriptional autorepressor. Distinct sequence and spacing requirements of the catalytic domain result in reduced cleavage activity on operator DNA. Crystallographic studies showed that the overall interactions of the DNA-binding domain with the operator and homing sites are similar, but have some different hydrogen-bonding contacts. We present a model in which the flexibility in protein-DNA interactions allows I-TevI to bind variant intronless alleles to promote intron mobility while facilitating its function in autorepression, and thereby persistence in its host. | Customary binding sites of intron-encoded homing endonucleases lie within cognate intronless alleles, at the so-called homing sites. Here, we describe a novel, high-affinity binding site for I-TevI endonuclease, encoded within the group I td intron of phage T4. This site is an operator that overlaps the T4 late promoter, which drives I-TevI expression from within the td intron. I-TevI binds the operator and homing sites with equal affinity, and functions as a transcriptional autorepressor. Distinct sequence and spacing requirements of the catalytic domain result in reduced cleavage activity on operator DNA. Crystallographic studies showed that the overall interactions of the DNA-binding domain with the operator and homing sites are similar, but have some different hydrogen-bonding contacts. We present a model in which the flexibility in protein-DNA interactions allows I-TevI to bind variant intronless alleles to promote intron mobility while facilitating its function in autorepression, and thereby persistence in its host. | ||
- | + | Intron-encoded homing endonuclease I-TevI also functions as a transcriptional autorepressor.,Edgell DR, Derbyshire V, Van Roey P, LaBonne S, Stanger MJ, Li Z, Boyd TM, Shub DA, Belfort M Nat Struct Mol Biol. 2004 Oct;11(10):936-44. Epub 2004 Sep 7. PMID:15361856<ref>PMID:15361856</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1t2t" style="background-color:#fffaf0;"></div> | |
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- | + | ==See Also== | |
+ | *[[Endonuclease 3D structures|Endonuclease 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Escherichia virus T4]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Belfort M]] | ||
+ | [[Category: Boyd TM]] | ||
+ | [[Category: Derbyshire V]] | ||
+ | [[Category: Edgell DR]] | ||
+ | [[Category: LaBonne S]] | ||
+ | [[Category: Li Z]] | ||
+ | [[Category: Shub DA]] | ||
+ | [[Category: Stanger MJ]] | ||
+ | [[Category: Van Roey P]] |
Current revision
Crystal structure of the DNA-binding domain of intron endonuclease I-TevI with operator site
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Categories: Escherichia virus T4 | Large Structures | Belfort M | Boyd TM | Derbyshire V | Edgell DR | LaBonne S | Li Z | Shub DA | Stanger MJ | Van Roey P