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1ln0

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(New page: 200px<br /><applet load="1ln0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ln0, resolution 2.0&Aring;" /> '''Structure of the Cata...)
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[[Image:1ln0.gif|left|200px]]<br /><applet load="1ln0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ln0, resolution 2.0&Aring;" />
 
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'''Structure of the Catalytic Domain of Homing Endonuclease I-TevI'''<br />
 
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==Overview==
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==Structure of the Catalytic Domain of Homing Endonuclease I-TevI==
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I-TevI, a member of the GIY-YIG family of homing endonucleases, consists, of an N-terminal catalytic domain and a C-terminal DNA-binding domain, joined by a flexible linker. The GIY-YIG motif is in the N-terminal domain, of I-TevI, which corresponds to a phylogenetically widespread catalytic, cartridge that is often associated with mobile genetic elements. The, crystal structure of the catalytic domain of I-TevI, the first of any, GIY-YIG endonuclease, reveals a novel alpha/beta-fold with a central, three-stranded antiparallel beta-sheet flanked by three helices. The most, conserved and putative catalytic residues are located on a shallow, concave surface and include a metal coordination site. Similarities in the, three-dimensional arrangement of the catalytically important residues and, the cation-binding site with those of the His-Cys box endonuclease I-PpoI, suggest the possibility of mechanistic relationships among these different, families of homing endonucleases despite completely different folds.
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<StructureSection load='1ln0' size='340' side='right'caption='[[1ln0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ln0]] is a 2 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=1LN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LN0 FirstGlance]. <br>
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ln0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ln0 OCA], [https://pdbe.org/1ln0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ln0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ln0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ln0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ln/1ln0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ln0 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1LN0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LN0 OCA].
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Catalytic domain structure and hypothesis for function of GIY-YIG intron endonuclease I-TevI., Van Roey P, Meehan L, Kowalski JC, Belfort M, Derbyshire V, Nat Struct Biol. 2002 Nov;9(11):806-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12379841 12379841]
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[[Category: Escherichia virus T4]]
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[[Category: Bacteriophage t4]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Belfort M]]
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[[Category: Belfort, M.]]
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[[Category: Derbyshire V]]
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[[Category: Derbyshire, V.]]
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[[Category: Kowalski JC]]
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[[Category: Kowalski, J.C.]]
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[[Category: Meehan L]]
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[[Category: Meehan, L.]]
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[[Category: Van Roey P]]
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[[Category: Roey, P.Van.]]
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[[Category: SO4]]
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[[Category: alpha/beta fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:41:19 2007''
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Current revision

Structure of the Catalytic Domain of Homing Endonuclease I-TevI

PDB ID 1ln0

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