3o48
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3o48 is ON HOLD Authors: Tooley, J.E., Khangulov, V., Heroux, A., Bosch, J., Hill, R.B. Description: Crystal structure of fission protein Fis1 from...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae== | |
| + | <StructureSection load='3o48' size='340' side='right'caption='[[3o48]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3o48]] is a 1 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=3O48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O48 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</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=3o48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o48 OCA], [https://pdbe.org/3o48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o48 RCSB], [https://www.ebi.ac.uk/pdbsum/3o48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o48 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fis1 mediates mitochondrial and peroxisomal fission. It is tail-anchored to these organelles by a transmembrane domain, exposing a soluble cytoplasmic domain. Previous studies suggested that Fis1 is autoinhibited by its N-terminal region. Here, a 1.75 A resolution crystal structure of the Fis1 cytoplasmic domain from Saccharomyces cerevisiae is reported which adopts a tetratricopeptide-repeat fold. It is observed that this fold creates a concave surface important for fission, but is sterically occluded by its N-terminal region. Thus, this structure provides a physical basis for autoinhibition and allows a detailed examination of the interactions that stabilize the inhibited state of this molecule. | ||
| - | + | The 1.75 A resolution structure of fission protein Fis1 from Saccharomyces cerevisiae reveals elusive interactions of the autoinhibitory domain.,Tooley JE, Khangulov V, Lees JP, Schlessman JL, Bewley MC, Heroux A, Bosch J, Hill RB Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt, 11):1310-5. Epub 2011 Oct 25. PMID:22102223<ref>PMID:22102223</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3o48" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Bosch J]] | ||
| + | [[Category: Heroux A]] | ||
| + | [[Category: Hill RB]] | ||
| + | [[Category: Khangulov V]] | ||
| + | [[Category: Tooley JE]] | ||
Current revision
Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae
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