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4TO7

N-Terminal domain of C. Reinhardtii SAS-6 homolog bld12p Q93E F145W K146R (NN24)

Summary for 4TO7
Entry DOI10.2210/pdb4to7/pdb
DescriptorCentriole protein (2 entities in total)
Functional Keywordssas-6, cartwheel, structural protein
Biological sourceChlamydomonas reinhardtii
Total number of polymer chains1
Total formula weight18171.65
Authors
Hilbert, M.,Kraatz, S.H.W. (deposition date: 2014-06-05, release date: 2015-06-17, Last modification date: 2023-12-20)
Primary citationHilbert, M.,Noga, A.,Frey, D.,Hamel, V.,Guichard, P.,Kraatz, S.H.,Pfreundschuh, M.,Hosner, S.,Fluckiger, I.,Jaussi, R.,Wieser, M.M.,Thieltges, K.M.,Deupi, X.,Muller, D.J.,Kammerer, R.A.,Gonczy, P.,Hirono, M.,Steinmetz, M.O.
SAS-6 engineering reveals interdependence between cartwheel and microtubules in determining centriole architecture.
Nat.Cell Biol., 18:393-403, 2016
Cited by
PubMed Abstract: Centrioles are critical for the formation of centrosomes, cilia and flagella in eukaryotes. They are thought to assemble around a nine-fold symmetric cartwheel structure established by SAS-6 proteins. Here, we have engineered Chlamydomonas reinhardtii SAS-6-based oligomers with symmetries ranging from five- to ten-fold. Expression of a SAS-6 mutant that forms six-fold symmetric cartwheel structures in vitro resulted in cartwheels and centrioles with eight- or nine-fold symmetries in vivo. In combination with Bld10 mutants that weaken cartwheel-microtubule interactions, this SAS-6 mutant produced six- to eight-fold symmetric cartwheels. Concurrently, the microtubule wall maintained eight- and nine-fold symmetries. Expressing SAS-6 with analogous mutations in human cells resulted in nine-fold symmetric centrioles that exhibited impaired length and organization. Together, our data suggest that the self-assembly properties of SAS-6 instruct cartwheel symmetry, and lead us to propose a model in which the cartwheel and the microtubule wall assemble in an interdependent manner to establish the native architecture of centrioles.
PubMed: 26999736
DOI: 10.1038/ncb3329
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.252 Å)
Structure validation

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数据于2024-11-06公开中

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