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| | ==Crystal Structure of Hof1p F-BAR domain== | | ==Crystal Structure of Hof1p F-BAR domain== |
| - | <StructureSection load='4wpe' size='340' side='right' caption='[[4wpe]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4wpe' size='340' side='right'caption='[[4wpe]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wpe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WPE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wpe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WPE FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.7Å</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=4wpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wpe OCA], [http://pdbe.org/4wpe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wpe RCSB], [http://www.ebi.ac.uk/pdbsum/4wpe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wpe ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4wpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wpe OCA], [https://pdbe.org/4wpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wpe RCSB], [https://www.ebi.ac.uk/pdbsum/4wpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wpe ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYK2_YEAST CYK2_YEAST]] Throughout most of the cell cycle it forms a double ring that coincides with the septins. After the onset of mitosis, forms a ring-like structure which colocalizes with the medial actin ring. Mediates cytoskeletal rearrangements required for cytokinesis. In conjunction with the medial actin ring exhibits contraction-like action.<ref>PMID:18344988</ref> <ref>PMID:19528296</ref> | + | [https://www.uniprot.org/uniprot/CYK2_YEAST CYK2_YEAST] Throughout most of the cell cycle it forms a double ring that coincides with the septins. After the onset of mitosis, forms a ring-like structure which colocalizes with the medial actin ring. Mediates cytoskeletal rearrangements required for cytokinesis. In conjunction with the medial actin ring exhibits contraction-like action.<ref>PMID:18344988</ref> <ref>PMID:19528296</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: Lemmon, M A]] | + | [[Category: Large Structures]] |
| - | [[Category: Moravcevic, K]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: F-bar domain]] | + | [[Category: Lemmon MA]] |
| - | [[Category: Membrane]] | + | [[Category: Moravcevic K]] |
| Structural highlights
Function
CYK2_YEAST Throughout most of the cell cycle it forms a double ring that coincides with the septins. After the onset of mitosis, forms a ring-like structure which colocalizes with the medial actin ring. Mediates cytoskeletal rearrangements required for cytokinesis. In conjunction with the medial actin ring exhibits contraction-like action.[1] [2]
Publication Abstract from PubMed
F-BAR domains control membrane interactions in endocytosis, cytokinesis, and cell signaling. Although they are generally thought to bind curved membranes containing negatively charged phospholipids, numerous functional studies argue that differences in lipid-binding selectivities of F-BAR domains are functionally important. Here, we compare membrane-binding properties of the Saccharomyces cerevisiae F-BAR domains in vitro and in vivo. Whereas some F-BAR domains (such as Bzz1p and Hof1p F-BARs) bind equally well to all phospholipids, the F-BAR domain from the RhoGAP Rgd1p preferentially binds phosphoinositides. We determined X-ray crystal structures of F-BAR domains from Hof1p and Rgd1p, the latter bound to an inositol phosphate. The structures explain phospholipid-binding selectivity differences and reveal an F-BAR phosphoinositide binding site that is fully conserved in a mammalian RhoGAP called Gmip and is partly retained in certain other F-BAR domains. Our findings reveal previously unappreciated determinants of F-BAR domain lipid-binding specificity and provide a basis for its prediction from sequence.
Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site.,Moravcevic K, Alvarado D, Schmitz KR, Kenniston JA, Mendrola JM, Ferguson KM, Lemmon MA Structure. 2015 Feb 3;23(2):352-63. doi: 10.1016/j.str.2014.12.009. Epub 2015 Jan, 22. PMID:25620000[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sanchez-Diaz A, Marchesi V, Murray S, Jones R, Pereira G, Edmondson R, Allen T, Labib K. Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast. Nat Cell Biol. 2008 Apr;10(4):395-406. doi: 10.1038/ncb1701. Epub 2008 Mar 16. PMID:18344988 doi:http://dx.doi.org/10.1038/ncb1701
- ↑ Nishihama R, Schreiter JH, Onishi M, Vallen EA, Hanna J, Moravcevic K, Lippincott MF, Han H, Lemmon MA, Pringle JR, Bi E. Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae. J Cell Biol. 2009 Jun 15;185(6):995-1012. PMID:19528296 doi:http://dx.doi.org/jcb.200903125
- ↑ Moravcevic K, Alvarado D, Schmitz KR, Kenniston JA, Mendrola JM, Ferguson KM, Lemmon MA. Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site. Structure. 2015 Feb 3;23(2):352-63. doi: 10.1016/j.str.2014.12.009. Epub 2015 Jan, 22. PMID:25620000 doi:http://dx.doi.org/10.1016/j.str.2014.12.009
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