1pc2: Difference between revisions

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-{{Seed}}
-[[Image:1pc2.png|left|200px]]
-<!--
+==Solution structure of human mitochondria fission protein Fis1==
-The line below this paragraph, containing "STRUCTURE_1pc2", creates the "Structure Box" on the page.
+<StructureSection load='1pc2' size='340' side='right'caption='[[1pc2]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1pc2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PC2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1pc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pc2 OCA], [https://pdbe.org/1pc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pc2 RCSB], [https://www.ebi.ac.uk/pdbsum/1pc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pc2 ProSAT]</span></td></tr>
-{{STRUCTURE_1pc2|  PDB=1pc2  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FIS1_HUMAN FIS1_HUMAN] Promotes the fragmentation of the mitochondrial network and its perinuclear clustering. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission.<ref>PMID:12783892</ref> <ref>PMID:12861026</ref> <ref>PMID:14996942</ref> <ref>PMID:16118244</ref> <ref>PMID:16107562</ref>
+== 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/pc/1pc2_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=1pc2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Fis1 in yeast localizes to the outer mitochondrial membrane and facilitates mitochondrial fission by forming protein complexes with Dnm1 and Mdv1. Fis1 orthologs exist in higher eukaryotes, suggesting that they are functionally conserved. In the present study, we cloned the human Fis1 ortholog that was predicted in a database, and determined the protein structure using NMR spectroscopy. Following a flexible N-terminal tail, six alpha-helices connected with short loops construct a single core domain. The C-terminal tail containing a transmembrane segment appears to be disordered. In the core domain, each of two sequentially adjacent helices forms a hairpin-like conformation, resulting in a six helix assembly forming a slightly twisted slab similar to that of a tandem array of tetratrico-peptide repeat (TPR) motif folds. Within this TPR-like core domain, no significant sequence similarity to the typical TPR motif is found. The structural analogy to the TPR-containing proteins suggests that Fis1 binds to other proteins at its concave hydrophobic surface. A simple composition of Fis1 comprised of a binding domain and a transmembrane segment indicates that the protein may function as a molecular adaptor on the mitochondrial outer membrane. In HeLa cells, however, increased levels in mitochondria-associated Fis1 did not result in mitochondrial translocation of Drp1, a potential binding partner of Fis1 implicated in the regulation of mitochondrial fission, suggesting that the interaction between Drp1 and Fis1 is regulated.
-===Solution structure of human mitochondria fission protein Fis1===
+The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle.,Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N J Mol Biol. 2003 Nov 28;334(3):445-58. PMID:14623186<ref>PMID:14623186</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_14623186}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1pc2" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 14623186 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14623186}}
+__TOC__
+</StructureSection>
-==About this Structure==
-PC2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC2 OCA].
-==Reference==
-The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle., Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N, J Mol Biol. 2003 Nov 28;334(3):445-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14623186 14623186]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Suzuki, M.]]
+[[Category: Suzuki M]]
-[[Category: Tjandra, N.]]
+[[Category: Tjandra N]]
-[[Category: Youle, R J.]]
+[[Category: Youle RJ]]
-[[Category: Fission]]
-[[Category: Mitochondria]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:58:43 2008''