|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of Septin 7 in complex with GDP== | | ==Crystal structure of Septin 7 in complex with GDP== |
| - | <StructureSection load='3t5d' size='340' side='right' caption='[[3t5d]], [[Resolution|resolution]] 3.30Å' scene=''> | + | <StructureSection load='3t5d' size='340' side='right'caption='[[3t5d]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3t5d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T5D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3t5d]] is a 2 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=3T5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T5D 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='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">SEPT7, CDC10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEPT7, CDC10 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3t5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5d OCA], [http://pdbe.org/3t5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t5d RCSB], [http://www.ebi.ac.uk/pdbsum/3t5d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t5d 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=3t5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5d OCA], [https://pdbe.org/3t5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t5d RCSB], [https://www.ebi.ac.uk/pdbsum/3t5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t5d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SEPT7_HUMAN SEPT7_HUMAN]] Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements.<ref>PMID:17803907</ref> <ref>PMID:18460473</ref> | + | [[https://www.uniprot.org/uniprot/SEPT7_HUMAN SEPT7_HUMAN]] Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements.<ref>PMID:17803907</ref> <ref>PMID:18460473</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 24: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Human]] | | [[Category: Human]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Wittinghofer, A]] | | [[Category: Wittinghofer, A]] |
| | [[Category: Zent, E]] | | [[Category: Zent, E]] |
| Structural highlights
Function
[SEPT7_HUMAN] Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements.[1] [2]
Publication Abstract from PubMed
Abstract Septins constitute a family of conserved guanine nucleotide binding proteins found in a wide range of organisms from fungi to mammals. Members of the family share a canonical G-domain with N- and C-terminal extensions. G-domains assemble into hetero-oligomeric complexes which form non-polarised filaments or rings. Linear filaments are formed between the G-domains using either the guanine nucleotide binding site (G interface) or N- and C-terminal extensions (NC interface). Sept7 is a unique among the 13 human septins in that it occupies the ends of hexameric building blocks which assemble into non-polarised filaments. To gain insight into its particular properties we performed structural and biochemical studies on Sept7. We solved the crystal structure of a Sept7 dimer in the GDP-bound state. The structure and biochemistry of Sept7 provide new insights into the dynamics of the G interface and outline the differences in the properties of Sept7 compared to the members of group 2 septins.
Structural and biochemical properties of Sept7, a unique septin required for filament formation.,Zent E, Vetter I, Wittinghofer A Biol Chem. 2011 Aug;392(8-9):791-7. PMID:21824007[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kremer BE, Adang LA, Macara IG. Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7. Cell. 2007 Sep 7;130(5):837-50. PMID:17803907 doi:http://dx.doi.org/10.1016/j.cell.2007.06.053
- ↑ Zhu M, Wang F, Yan F, Yao PY, Du J, Gao X, Wang X, Wu Q, Ward T, Li J, Kioko S, Hu R, Xie W, Ding X, Yao X. Septin 7 interacts with centromere-associated protein E and is required for its kinetochore localization. J Biol Chem. 2008 Jul 4;283(27):18916-25. doi: 10.1074/jbc.M710591200. Epub 2008 , May 6. PMID:18460473 doi:http://dx.doi.org/10.1074/jbc.M710591200
- ↑ Zent E, Vetter I, Wittinghofer A. Structural and biochemical properties of Sept7, a unique septin required for filament formation. Biol Chem. 2011 Aug;392(8-9):791-7. PMID:21824007 doi:10.1515/BC.2011.082
|
