1vde

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[[Image:1vde.gif|left|200px]]
 
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{{Structure
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==PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY==
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|PDB= 1vde |SIZE=350|CAPTION= <scene name='initialview01'>1vde</scene>, resolution 2.4&Aring;
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<StructureSection load='1vde' size='340' side='right'caption='[[1vde]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1vde]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VDE FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span>
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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]] 2.4&#8491;</td></tr>
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|GENE=
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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=1vde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vde OCA], [https://pdbe.org/1vde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vde RCSB], [https://www.ebi.ac.uk/pdbsum/1vde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vde ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vde OCA], [http://www.ebi.ac.uk/pdbsum/1vde PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vde RCSB]</span>
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[https://www.uniprot.org/uniprot/VATA_YEAST VATA_YEAST] Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit.<ref>PMID:1534148</ref> PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates "homing", a genetic event that converts a VMA1 allele lacking VDE into one that contains it.<ref>PMID:1534148</ref>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY'''
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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/vd/1vde_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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PI-Scel is a bifunctional yeast protein that propagates its mobile gene by catalyzing protein splicing and site-specific DNA double-strand cleavage. Here, we report the 2.4 A crystal structure of the PI-Scel protein. The structure is composed of two separate domains (I and II) with novel folds and different functions. Domain I, which is elongated and formed largely from seven beta sheets, harbors the N and C termini residues and two His residues that are implicated in protein splicing. Domain II, which is compact and is primarily composed of two similar alpha/beta motifs related by local two-fold symmetry, contains the putative nuclease active site with a cluster of two acidic residues and one basic residue commonly found in restriction endonucleases. This report presents prototypic structures of domains with single endonuclease and protein splicing active sites.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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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=1vde ConSurf].
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1VDE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VDE OCA].
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<div style="clear:both"></div>
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== References ==
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==Reference==
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<references/>
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Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity., Duan X, Gimble FS, Quiocho FA, Cell. 1997 May 16;89(4):555-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9160747 9160747]
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__TOC__
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[[Category: H(+)-transporting two-sector ATPase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Duan X]]
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[[Category: Duan, X.]]
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[[Category: Quiocho FA]]
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[[Category: Quiocho, F A.]]
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[[Category: homing endonuclease]]
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[[Category: protein splicing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:22:52 2008''
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PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY

PDB ID 1vde

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