1mk0

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Current revision (08:37, 10 April 2024) (edit) (undo)
 
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<StructureSection load='1mk0' size='340' side='right'caption='[[1mk0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1mk0' size='340' side='right'caption='[[1mk0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1mk0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MK0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1mk0]] is a 1 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=1MK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MK0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
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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]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ln0|1ln0]]</div></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=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=1mk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mk0 OCA], [https://pdbe.org/1mk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mk0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mk0 ProSAT]</span></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=1mk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mk0 OCA], [https://pdbe.org/1mk0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mk0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mk0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mk0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1mk0 ConSurf].
</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=1mk0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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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:12379841<ref>PMID:12379841</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1mk0" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bpt4]]
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[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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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, J C]]
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[[Category: Kowalski JC]]
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[[Category: Meehan, L]]
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[[Category: Meehan L]]
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[[Category: Roey, P Van]]
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[[Category: Van Roey P]]
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[[Category: Alpha/beta fold]]
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[[Category: Catalytic domain]]
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[[Category: Dna-binding surface]]
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[[Category: Hydrolase]]
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Current revision

catalytic domain of intron endonuclease I-TevI, E75A mutant

PDB ID 1mk0

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