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| | <StructureSection load='6mqk' size='340' side='right'caption='[[6mqk]], [[Resolution|resolution]] 2.19Å' scene=''> | | <StructureSection load='6mqk' size='340' side='right'caption='[[6mqk]], [[Resolution|resolution]] 2.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mqk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MQK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mqk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MQK FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.19Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEPT12 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6mqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mqk OCA], [https://pdbe.org/6mqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mqk RCSB], [https://www.ebi.ac.uk/pdbsum/6mqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mqk 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=6mqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mqk OCA], [https://pdbe.org/6mqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mqk RCSB], [https://www.ebi.ac.uk/pdbsum/6mqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mqk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/SEP12_HUMAN SEP12_HUMAN]] Non-syndromic male infertility due to sperm motility disorder. The disease is caused by mutations affecting the gene represented in this entry.
| + | [https://www.uniprot.org/uniprot/SEP12_HUMAN SEP12_HUMAN] Non-syndromic male infertility due to sperm motility disorder. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SEP12_HUMAN SEP12_HUMAN]] Filament-forming cytoskeletal GTPase (By similarity). Involved in spermatogenesis. Involved in the morphogenesis of sperm heads and the elongation of sperm tails probably implicating the association with alpha- and beta-tubulins (PubMed:24213608). Forms a filamentous structure with SEPTIN7, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (PubMed:25588830). May play a role in cytokinesis (Potential).<ref>PMID:24213608</ref> <ref>PMID:25588830</ref>
| + | [https://www.uniprot.org/uniprot/SEP12_HUMAN SEP12_HUMAN] Filament-forming cytoskeletal GTPase (By similarity). Involved in spermatogenesis. Involved in the morphogenesis of sperm heads and the elongation of sperm tails probably implicating the association with alpha- and beta-tubulins (PubMed:24213608). Forms a filamentous structure with SEPTIN7, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (PubMed:25588830). May play a role in cytokinesis (Potential).<ref>PMID:24213608</ref> <ref>PMID:25588830</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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brandao-Neto, J]] | + | [[Category: Brandao-Neto J]] |
| - | [[Category: Castro, D K.S V]] | + | [[Category: Castro DKSV]] |
| - | [[Category: Garratt, R C]] | + | [[Category: Garratt RC]] |
| - | [[Category: Pereira, H M]] | + | [[Category: Pereira HM]] |
| - | [[Category: Ulian, A P.U]] | + | [[Category: Ulian APU]] |
| - | [[Category: Cytoskeleton component septin gtpase spermatogenesis]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Disease
SEP12_HUMAN Non-syndromic male infertility due to sperm motility disorder. The disease is caused by mutations affecting the gene represented in this entry.
Function
SEP12_HUMAN Filament-forming cytoskeletal GTPase (By similarity). Involved in spermatogenesis. Involved in the morphogenesis of sperm heads and the elongation of sperm tails probably implicating the association with alpha- and beta-tubulins (PubMed:24213608). Forms a filamentous structure with SEPTIN7, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (PubMed:25588830). May play a role in cytokinesis (Potential).[1] [2]
Publication Abstract from PubMed
Human septins 3, 9 and 12 are the only members of a specific subgroup of septins that display several unusual features, including the absence of a C-terminal coiled coil. This particular subgroup (the SEPT3 septins) are present in rod-like octameric protofilaments but are lacking in similar hexameric assemblies, which only contain representatives of the three remaining subgroups. Both hexamers and octamers can self-assemble into mixed filaments by end-to-end association, implying that the SEPT3 septins may facilitate polymerization but not necessarily function. These filaments frequently associate into higher order complexes which associate with biological membranes, triggering a wide range of cellular events. In the present work, a complete compendium of crystal structures for the GTP-binding domains of all of the SEPT3 subgroup members when bound to either GDP or to a GTP analogue is provided. The structures reveal a unique degree of plasticity at one of the filamentous interfaces (dubbed NC). Specifically, structures of the GDP and GTPgammaS complexes of SEPT9 reveal a squeezing mechanism at the NC interface which would expel a polybasic region from its binding site and render it free to interact with negatively charged membranes. On the other hand, a polyacidic region associated with helix alpha5', the orientation of which is particular to this subgroup, provides a safe haven for the polybasic region when retracted within the interface. Together, these results suggest a mechanism which couples GTP binding and hydrolysis to membrane association and implies a unique role for the SEPT3 subgroup in this process. These observations can be accounted for by constellations of specific amino-acid residues that are found only in this subgroup and by the absence of the C-terminal coiled coil. Such conclusions can only be reached owing to the completeness of the structural studies presented here.
A complete compendium of crystal structures for the human SEPT3 subgroup reveals functional plasticity at a specific septin interface.,Castro DKSDV, da Silva SMO, Pereira HD, Macedo JNA, Leonardo DA, Valadares NF, Kumagai PS, Brandao-Neto J, Araujo APU, Garratt RC IUCrJ. 2020 Mar 28;7(Pt 3):462-479. doi: 10.1107/S2052252520002973. eCollection, 2020 May 1. PMID:32431830[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kuo PL, Chiang HS, Wang YY, Kuo YC, Chen MF, Yu IS, Teng YN, Lin SW, Lin YH. SEPT12-microtubule complexes are required for sperm head and tail formation. Int J Mol Sci. 2013 Nov 7;14(11):22102-16. doi: 10.3390/ijms141122102. PMID:24213608 doi:http://dx.doi.org/10.3390/ijms141122102
- ↑ Kuo YC, Shen YR, Chen HI, Lin YH, Wang YY, Chen YR, Wang CY, Kuo PL. SEPT12 orchestrates the formation of mammalian sperm annulus by organizing core octameric complexes with other SEPT proteins. J Cell Sci. 2015 Mar 1;128(5):923-34. doi: 10.1242/jcs.158998. Epub 2015 Jan 14. PMID:25588830 doi:http://dx.doi.org/10.1242/jcs.158998
- ↑ Castro DKSDV, da Silva SMO, Pereira HD, Macedo JNA, Leonardo DA, Valadares NF, Kumagai PS, Brandao-Neto J, Araujo APU, Garratt RC. A complete compendium of crystal structures for the human SEPT3 subgroup reveals functional plasticity at a specific septin interface. IUCrJ. 2020 Mar 28;7(Pt 3):462-479. doi: 10.1107/S2052252520002973. eCollection, 2020 May 1. PMID:32431830 doi:http://dx.doi.org/10.1107/S2052252520002973
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