4YV4

Structure of the C. elegans SAS-5 coiled coil domain

Summary for 4YV4

• Entry DOI: 10.2210/pdb4yv4/pdb
• Related: 4YNH
• Descriptor: Spindle assembly abnormal protein 5, PHOSPHATE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: structural protein, coiled coil, trimer, a-helical, cell cycle
• Biological source: Caenorhabditis elegans
• Cellular location: Cytoplasm: Q20010
• Total number of polymer chains: 8
• Total formula weight: 55483.42

Authors

Rogala, K.B.,Hatzopoulos, G.N.,Vakonakis, I. (deposition date: 2015-03-19, release date: 2015-06-10, Last modification date: 2024-05-08)

Primary citation

Rogala, K.B.,Dynes, N.J.,Hatzopoulos, G.N.,Yan, J.,Pong, S.K.,Robinson, C.V.,Deane, C.M.,Gonczy, P.,Vakonakis, I.
The Caenorhabditis elegans protein SAS-5 forms large oligomeric assemblies critical for centriole formation.
Elife, 4:e07410-e07410, 2015

PubMed Abstract: Centrioles are microtubule-based organelles crucial for cell division, sensing and motility. In Caenorhabditis elegans, the onset of centriole formation requires notably the proteins SAS-5 and SAS-6, which have functional equivalents across eukaryotic evolution. Whereas the molecular architecture of SAS-6 and its role in initiating centriole formation are well understood, the mechanisms by which SAS-5 and its relatives function is unclear. Here, we combine biophysical and structural analysis to uncover the architecture of SAS-5 and examine its functional implications in vivo. Our work reveals that two distinct self-associating domains are necessary to form higher-order oligomers of SAS-5: a trimeric coiled coil and a novel globular dimeric Implico domain. Disruption of either domain leads to centriole duplication failure in worm embryos, indicating that large SAS-5 assemblies are necessary for function in vivo.

PubMed: 26023830
DOI: 10.7554/eLife.07410

Experimental method

X-RAY DIFFRACTION (1.8 Å)