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4G79

Structure a C. elegans SAS-6 variant

Summary for 4G79
Entry DOI10.2210/pdb4g79/pdb
Related2Y3V 2Y3W 3PYI 3Q0X 3Q0Y
DescriptorSpindle assembly abnormal protein 6, GLYCEROL, TETRAETHYLENE GLYCOL, ... (4 entities in total)
Functional Keywordsstructural protein, beta-sandwich, alpha-beta protein, cytoplasmic, centriolar, centriole, central tube
Biological sourceCaenorhabditis elegans (nematode)
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Cellular locationCytoplasm: O62479
Total number of polymer chains1
Total formula weight17127.65
Authors
Erat, M.C.,Vakonakis, I. (deposition date: 2012-07-20, release date: 2013-06-19, Last modification date: 2024-10-30)
Primary citationHilbert, M.,Erat, M.C.,Hachet, V.,Guichard, P.,Blank, I.D.,Fluckiger, I.,Slater, L.,Lowe, E.D.,Hatzopoulos, G.N.,Steinmetz, M.O.,Gonczy, P.,Vakonakis, I.
Caenorhabditis elegans centriolar protein SAS-6 forms a spiral that is consistent with imparting a ninefold symmetry.
Proc.Natl.Acad.Sci.USA, 110:11373-11378, 2013
Cited by
PubMed Abstract: Centrioles are evolutionary conserved organelles that give rise to cilia and flagella as well as centrosomes. Centrioles display a characteristic ninefold symmetry imposed by the spindle assembly abnormal protein 6 (SAS-6) family. SAS-6 from Chlamydomonas reinhardtii and Danio rerio was shown to form ninefold symmetric, ring-shaped oligomers in vitro that were similar to the cartwheels observed in vivo during early steps of centriole assembly in most species. Here, we report crystallographic and EM analyses showing that, instead, Caenorhabotis elegans SAS-6 self-assembles into a spiral arrangement. Remarkably, we find that this spiral arrangement is also consistent with ninefold symmetry, suggesting that two distinct SAS-6 oligomerization architectures can direct the same output symmetry. Sequence analysis suggests that SAS-6 spirals are restricted to specific nematodes. This oligomeric arrangement may provide a structural basis for the presence of a central tube instead of a cartwheel during centriole assembly in these species.
PubMed: 23798409
DOI: 10.1073/pnas.1302721110
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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数据于2024-11-06公开中

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