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| | ==GTPase domain of Septin 10 from Schistosoma mansoni in complex with GDP== | | ==GTPase domain of Septin 10 from Schistosoma mansoni in complex with GDP== |
| - | <StructureSection load='4kv9' size='340' side='right' caption='[[4kv9]], [[Resolution|resolution]] 1.93Å' scene=''> | + | <StructureSection load='4kv9' size='340' side='right'caption='[[4kv9]], [[Resolution|resolution]] 1.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kv9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KV9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KV9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kv9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KV9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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]] 1.93Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kva|4kva]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Septin 10, Smp_029890 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6183 Blood fluke])</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=4kv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kv9 OCA], [https://pdbe.org/4kv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kv9 RCSB], [https://www.ebi.ac.uk/pdbsum/4kv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kv9 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=4kv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kv9 OCA], [http://pdbe.org/4kv9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kv9 RCSB], [http://www.ebi.ac.uk/pdbsum/4kv9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kv9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SEP10_SCHMA SEP10_SCHMA] Filament-forming GTP-binding protein. Lacks GTPase activity, which is likely due to absence of an essential threonine residue important for hydrolytic activity in septins. May be involved in membrane remodeling, potentially by its nucleotide-dependent cellular membrane association/dissociation ability (PubMed:24464615). Able to bind to phosphatidylinositol-4,5-bisphosphate (PIP2)-containing giant unilamellar vesicles (GUVs), which serve as a model of biological membranes. Self-assembles into ordered cage-like structures on the vesicle membrane. Binds also to 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS)-containing vesicles suggesting the requirement for negatively charged membranes. Is also able to promote deformation of the GUVs (PubMed:27687162).<ref>PMID:24464615</ref> <ref>PMID:27687162</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: Blood fluke]] | + | [[Category: Large Structures]] |
| - | [[Category: Araujo, A P.U]] | + | [[Category: Schistosoma mansoni]] |
| - | [[Category: Brandao-Neto, J]] | + | [[Category: Araujo APU]] |
| - | [[Category: Demarco, R]] | + | [[Category: Brandao-Neto J]] |
| - | [[Category: Garratt, R C]] | + | [[Category: Demarco R]] |
| - | [[Category: Pereira, H M]] | + | [[Category: Garratt RC]] |
| - | [[Category: Santos, Y V]] | + | [[Category: Pereira HM]] |
| - | [[Category: Zeraik, A E]] | + | [[Category: Santos YV]] |
| - | [[Category: Cytoskeleton component]]
| + | [[Category: Zeraik AE]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Septin]]
| + | |
| - | [[Category: Small gtpase]]
| + | |
| Structural highlights
Function
SEP10_SCHMA Filament-forming GTP-binding protein. Lacks GTPase activity, which is likely due to absence of an essential threonine residue important for hydrolytic activity in septins. May be involved in membrane remodeling, potentially by its nucleotide-dependent cellular membrane association/dissociation ability (PubMed:24464615). Able to bind to phosphatidylinositol-4,5-bisphosphate (PIP2)-containing giant unilamellar vesicles (GUVs), which serve as a model of biological membranes. Self-assembles into ordered cage-like structures on the vesicle membrane. Binds also to 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS)-containing vesicles suggesting the requirement for negatively charged membranes. Is also able to promote deformation of the GUVs (PubMed:27687162).[1] [2]
Publication Abstract from PubMed
Septins are filament forming GTP-binding proteins involved in important cellular events such as cytokinesis, barrier formation and membrane remodeling. Here, we present two crystal structures of the GTPase domain of a Schistosoma mansoni septin (SmSEPT10); one bound to GDP and the other to GTP. The structures have been solved at an unprecedented resolution for septins (1.93 and 2.1 A respectively) which has allowed for unambiguous structural assignment of regions previously poorly defined. Consequently we provide a reliable model for functional interpretation and a solid foundation for future structural studies. On comparing the two complexes, we observe for the first time the phenomenon of a strand slippage in septins. Such slippage generates a front-back communication mechanism between the G and NC interfaces. This data provides a novel mechanistic framework for the influence of nucleotide binding to the GTPase domain, opening new possibilities for the study of the dynamics of septin filaments.
Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide.,Zeraik AE, Pereira HM, Santos YV, Brandao-Neto J, Spoerner M, Santos MS, Colnago LA, Garratt RC, Araujo AP, Demarco R J Biol Chem. 2014 Jan 24. PMID:24464615[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zeraik AE, Pereira HM, Santos YV, Brandao-Neto J, Spoerner M, Santos MS, Colnago LA, Garratt RC, Araujo AP, Demarco R. Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide. J Biol Chem. 2014 Jan 24. PMID:24464615 doi:http://dx.doi.org/10.1074/jbc.M113.525352
- ↑ Zeraik AE, Staykova M, Fontes MG, Nemuraite I, Quinlan R, Araujo AP, DeMarco R. Biophysical dissection of schistosome septins: Insights into oligomerization and membrane binding. Biochimie. 2016 Dec;131:96-105. doi: 10.1016/j.biochi.2016.09.014. Epub 2016 Sep , 26. PMID:27687162 doi:http://dx.doi.org/10.1016/j.biochi.2016.09.014
- ↑ Zeraik AE, Pereira HM, Santos YV, Brandao-Neto J, Spoerner M, Santos MS, Colnago LA, Garratt RC, Araujo AP, Demarco R. Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide. J Biol Chem. 2014 Jan 24. PMID:24464615 doi:http://dx.doi.org/10.1074/jbc.M113.525352
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