2pqr

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[[Image:2pqr.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of yeast Fis1 complexed with a fragment of yeast Caf4==
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|PDB= 2pqr |SIZE=350|CAPTION= <scene name='initialview01'>2pqr</scene>, resolution 1.880&Aring;
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<StructureSection load='2pqr' size='340' side='right'caption='[[2pqr]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=AU:GOLD ION'>AU</scene>
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<table><tr><td colspan='2'>[[2pqr]] is a 4 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=2PQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQR FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.88&#8491;</td></tr>
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|GENE= FIS1, MDV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), CAF4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></td></tr>
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}}
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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=2pqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqr OCA], [https://pdbe.org/2pqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqr RCSB], [https://www.ebi.ac.uk/pdbsum/2pqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FIS1_YEAST FIS1_YEAST] Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division.<ref>PMID:11038183</ref> <ref>PMID:11038182</ref> <ref>PMID:12163467</ref> <ref>PMID:12679388</ref>
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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/pq/2pqr_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=2pqr ConSurf].
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<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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Mitochondrial fission controls mitochondrial shape and physiology, including mitochondrial remodeling in apoptosis. During assembly of the yeast mitochondrial fission complex, the outer membrane protein Fis1 recruits the dynamin-related GTPase Dnm1 to mitochondria. Fis1 contains a tetratricopeptide repeat (TPR) domain and interacts with Dnm1 via the molecular adaptors Mdv1 and Caf4. By using crystallographic analysis of adaptor-Fis1 complexes, we show that these adaptors use two helices to bind to both the concave and convex surfaces of the Fis1 TPR domain. Fis1 therefore contains two interaction interfaces, a binding mode that, to our knowledge, has not been observed previously for TPR domains. Genetic and biochemical studies indicate that both binding interfaces are important for binding of Mdv1 and Caf4 to Fis1 and for mitochondrial fission activity in vivo. Our results reveal how Fis1 recruits the mitochondrial fission complex and will facilitate efforts to manipulate mitochondrial fission.
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'''Crystal structure of yeast Fis1 complexed with a fragment of yeast Caf4'''
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Structural basis for recruitment of mitochondrial fission complexes by Fis1.,Zhang Y, Chan DC Proc Natl Acad Sci U S A. 2007 Nov 20;104(47):18526-30. Epub 2007 Nov 12. PMID:17998537<ref>PMID:17998537</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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==About this Structure==
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</div>
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2PQR is a [[Protein complex]] structure of sequences 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=2PQR OCA].
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<div class="pdbe-citations 2pqr" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Chan, D C.]]
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[[Category: Chan DC]]
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[[Category: Zhang, Y.]]
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[[Category: Zhang Y]]
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[[Category: AU]]
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[[Category: apoptosis]]
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[[Category: protein-protein complex]]
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[[Category: tpr domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:17 2008''
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Current revision

Crystal structure of yeast Fis1 complexed with a fragment of yeast Caf4

PDB ID 2pqr

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