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==Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae==
==Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae==
<StructureSection load='3o48' size='340' side='right' caption='[[3o48]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='3o48' size='340' side='right'caption='[[3o48]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o48]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O48 FirstGlance]. <br>
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y8m|1y8m]], [[2pqn|2pqn]], [[2pqr|2pqr]], [[1nzn|1nzn]], [[1iyg|1iyg]], [[1pc2|1pc2]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FIS1, MDV2, YIL065C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o48 OCA], [http://pdbe.org/3o48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o48 RCSB], [http://www.ebi.ac.uk/pdbsum/3o48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o48 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Bosch, J]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Heroux, A]]
[[Category: Bosch J]]
[[Category: Hill, R B]]
[[Category: Heroux A]]
[[Category: Khangulov, V]]
[[Category: Hill RB]]
[[Category: Tooley, J E]]
[[Category: Khangulov V]]
[[Category: Membrane fission]]
[[Category: Tooley JE]]
[[Category: Mitochondria]]
[[Category: Peroxisome]]
[[Category: Protein binding]]
[[Category: Scaffold]]
[[Category: Tetratricopeptide repeat fold]]
[[Category: Tpr]]

Latest revision as of 12:27, 6 September 2023

Crystal structure of fission protein Fis1 from Saccharomyces cerevisiaeCrystal structure of fission protein Fis1 from Saccharomyces cerevisiae

Structural highlights

3o48 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

3o48, resolution 1.75Å

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