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| - | [[Image:3o48.png|left|200px]] | |
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| - | <!-- | + | ==Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae== |
| - | The line below this paragraph, containing "STRUCTURE_3o48", creates the "Structure Box" on the page.
| + | <StructureSection load='3o48' size='340' side='right'caption='[[3o48]], [[Resolution|resolution]] 1.75Å' 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'>[[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> |
| - | 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">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> |
| - | {{STRUCTURE_3o48| PDB=3o48 | SCENE= }}
| + | </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. |
| | | | |
| - | ===Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae===
| + | 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> |
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| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <!--
| + | </div> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_22102223}}, adds the Publication Abstract to the page
| + | <div class="pdbe-citations 3o48" style="background-color:#fffaf0;"></div> |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 22102223 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_22102223}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Large Structures]] |
| - | [[3o48]] is a 1 chain structure with 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=3O48 OCA].
| + | |
| - | | + | |
| - | ==Reference== | + | |
| - | <ref group="xtra">PMID:022102223</ref><references group="xtra"/> | + | |
| | [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Bosch, J.]] | + | [[Category: Bosch J]] |
| - | [[Category: Heroux, A.]] | + | [[Category: Heroux A]] |
| - | [[Category: Hill, R B.]] | + | [[Category: Hill RB]] |
| - | [[Category: Khangulov, V.]] | + | [[Category: Khangulov V]] |
| - | [[Category: Tooley, J E.]] | + | [[Category: Tooley JE]] |
| - | [[Category: Membrane fission]]
| + | |
| - | [[Category: Mitochondria]]
| + | |
| - | [[Category: Peroxisome]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Scaffold]]
| + | |
| - | [[Category: Tetratricopeptide repeat fold]]
| + | |
| - | [[Category: Tpr]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4]
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mozdy AD, McCaffery JM, Shaw JM. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J Cell Biol. 2000 Oct 16;151(2):367-80. PMID:11038183
- ↑ Tieu Q, Nunnari J. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J Cell Biol. 2000 Oct 16;151(2):353-66. PMID:11038182
- ↑ Tieu Q, Okreglak V, Naylor K, Nunnari J. The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J Cell Biol. 2002 Aug 5;158(3):445-52. Epub 2002 Aug 5. PMID:12163467 doi:http://dx.doi.org/10.1083/jcb.200205031
- ↑ Jakobs S, Martini N, Schauss AC, Egner A, Westermann B, Hell SW. Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p. J Cell Sci. 2003 May 15;116(Pt 10):2005-14. Epub 2003 Apr 1. PMID:12679388 doi:http://dx.doi.org/10.1242/jcs.00423
- ↑ Tooley JE, Khangulov V, Lees JP, Schlessman JL, Bewley MC, Heroux A, Bosch J, Hill RB. The 1.75 A resolution structure of fission protein Fis1 from Saccharomyces cerevisiae reveals elusive interactions of the autoinhibitory domain. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt, 11):1310-5. Epub 2011 Oct 25. PMID:22102223 doi:10.1107/S1744309111029368
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