1mk0

<StructureSection load='1mk0' size='340' side='right' caption='[[1mk0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[1mk0]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MK0 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ln0|1ln0]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mk0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mk0 OCA], [http://pdbe.org/1mk0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mk0 RCSB], [http://www.ebi.ac.uk/pdbsum/1mk0 PDBsum]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mk/1mk0_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1mk0" style="background-color:#fffaf0;"></div>

*[[Endonuclease|Endonuclease]]

[[Category: Bpt4]]

[[Category: Belfort, M]]

[[Category: Derbyshire, V]]

[[Category: Kowalski, J C]]

[[Category: Meehan, L]]

[[Category: Roey, P Van]]

[[Category: Hydrolase]]