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| | <StructureSection load='6oec' size='340' side='right'caption='[[6oec]], [[Resolution|resolution]] 2.51Å' scene=''> | | <StructureSection load='6oec' size='340' side='right'caption='[[6oec]], [[Resolution|resolution]] 2.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6oec]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Carhz Carhz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OEC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6oec]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans_Z-2901 Carboxydothermus hydrogenoformans Z-2901] and [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=6OEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OEC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.514Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPC42, YKL042W, YKL255 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246194 CARHZ])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=6oec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oec OCA], [http://pdbe.org/6oec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oec RCSB], [http://www.ebi.ac.uk/pdbsum/6oec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oec ProSAT]</span></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=6oec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oec OCA], [https://pdbe.org/6oec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oec RCSB], [https://www.ebi.ac.uk/pdbsum/6oec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oec ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SPC42_YEAST SPC42_YEAST] Forms a polymeric layer at the periphery of the spindle pole body (SPB) central plaque which has an essential function during SPB duplication and may facilitate attachment of the SPB to the nuclear membrane.<ref>PMID:10339566</ref> [https://www.uniprot.org/uniprot/Q3ADQ4_CARHZ Q3ADQ4_CARHZ] |
| | <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: Carhz]] | + | [[Category: Carboxydothermus hydrogenoformans Z-2901]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andreas, M P]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Drennan, A C]] | + | [[Category: Andreas MP]] |
| - | [[Category: Gardner, J M]] | + | [[Category: Drennan AC]] |
| - | [[Category: Jasperson, S L]] | + | [[Category: Gardner JM]] |
| - | [[Category: Rayment, I]] | + | [[Category: Jasperson SL]] |
| - | [[Category: Seeger, M A]] | + | [[Category: Rayment I]] |
| - | [[Category: Sether, E K.R]] | + | [[Category: Seeger MA]] |
| - | [[Category: Shivaani, K]] | + | [[Category: Sether EKR]] |
| - | [[Category: Spindle pole body]]
| + | [[Category: Shivaani K]] |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Trimeric coiled-coil]]
| + | |
| - | [[Category: Yeast centrosome]]
| + | |
| Structural highlights
Function
SPC42_YEAST Forms a polymeric layer at the periphery of the spindle pole body (SPB) central plaque which has an essential function during SPB duplication and may facilitate attachment of the SPB to the nuclear membrane.[1] Q3ADQ4_CARHZ
Publication Abstract from PubMed
Centrosomes and spindle pole bodies (SPBs) are membraneless organelles whose duplication and assembly is necessary for bipolar mitotic spindle formation. The structural organization and functional roles of major proteins in these organelles can provide critical insights into cell division control. Spc42, a phosphoregulated protein with an N-terminal dimeric coiled-coil, assembles into a hexameric array at the budding yeast SPB core, where it functions as a scaffold for SPB assembly. Here, we present in vitro and in vivo data to elucidate the structural arrangement and biological roles of Spc42 elements. Crystal structures reveal details of two additional coiled-coils in Spc42: a central trimeric coiled-coil and a C-terminal antiparallel dimeric coiled-coil. Contributions of the three Spc42 coiled-coils and adjacent undetermined regions to the formation of a approximately 145 A hexameric lattice in an in vitro lipid monolayer assay, and to SPB duplication and assembly in vivo, reveal structural and functional redundancy in Spc42 assembly. We propose an updated model that incorporates the inherent symmetry of these Spc42 elements into a lattice, and thereby establishes the observed six-fold symmetry. The implications of this model for the organization of the central SPB core layer are discussed.
Structure and function of Spc42 coiled-coils in yeast centrosome assembly and duplication.,Drennan AC, Krishna S, Seeger MA, Andreas MP, Gardner JM, Sether EKR, Jaspersen SL, Rayment I Mol Biol Cell. 2019 Apr 10:mbcE19030167. doi: 10.1091/mbc.E19-03-0167. PMID:30969903[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Elliott S, Knop M, Schlenstedt G, Schiebel E. Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication. Proc Natl Acad Sci U S A. 1999 May 25;96(11):6205-10. PMID:10339566
- ↑ Drennan AC, Krishna S, Seeger MA, Andreas MP, Gardner JM, Sether EKR, Jaspersen SL, Rayment I. Structure and function of Spc42 coiled-coils in yeast centrosome assembly and duplication. Mol Biol Cell. 2019 Apr 10:mbcE19030167. doi: 10.1091/mbc.E19-03-0167. PMID:30969903 doi:http://dx.doi.org/10.1091/mbc.E19-03-0167
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