Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9QZC

Proximal A-C linker of Tetrahymena centriole, one repeating unit

This is a non-PDB format compatible entry.
Summary for 9QZC
Entry DOI10.2210/pdb9qzc/pdb
EMDB information53467
DescriptorWD repeat WRAP73-like protein, putative, Unknown Protein Chain, Centrosomal protein, putative, ... (15 entities in total)
Functional Keywordscentriole, basal body, centrosome, structural protein
Biological sourceTetrahymena thermophila
More
Total number of polymer chains18
Total formula weight757563.27
Authors
Cai, B.,Xu, J.W.,Luo, L.,Aarts, E.,Leitner, A.,Ishikawa, T.,Beltro, P.,Pilhofer, M.,Wieczorek, M. (deposition date: 2025-04-22, release date: 2025-09-17, Last modification date: 2025-10-22)
Primary citationCai, B.,Xu, J.,Collet, E.H.,Aarts, E.,Luo, L.,Leitner, A.,Ishikawa, T.,Beltrao, P.,Pearson, C.G.,Pilhofer, M.,Wieczorek, M.
Structure and assembly of the A-C linker connecting microtubule triplets in centrioles.
Sci Adv, 11:eady3689-eady3689, 2025
Cited by
PubMed Abstract: Centriole assembly involves the coordination of centriolar modules. One module is the A-C linker, an enigmatic protein assembly connecting the A-microtubule of one microtubule triplet to the C-microtubule of the neighboring triplet. Here, we integrated biochemistry, multiscale cryo-electron microscopy, and AlphaFold modeling to investigate the architecture of the centriole. Using an improved centriole isolation method, we determined the structure of the A-C linker bound to microtubule triplets, which revealed how the A-C linker cross-links microtubules and integrates with the B-C junction. We found marked changes in the structure and composition of the A-C linker that correlate with the presence of other centriolar modules, including the pinhead, cartwheel, and inner scaffold. Our findings show that the A-C linker is a highly integrated component of the centriole whose polymorphism may orchestrate the assembly of spatially distinct centriolar modules, and provide a framework for dissecting the biology of centrioles.
PubMed: 41061066
DOI: 10.1126/sciadv.ady3689
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

247035

PDB entries from 2026-01-07

PDB statisticsPDBj update infoContact PDBjnumon