Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7N6G

C1 of central pair

This is a non-PDB format compatible entry.
Summary for 7N6G
Entry DOI10.2210/pdb7n6g/pdb
EMDB information24207
DescriptorPF16, FAP108, FAP76, ... (54 entities in total)
Functional Keywordscentral pair, structural protein
Biological sourceChlamydomonas reinhardtii
More
Total number of polymer chains264
Total formula weight16146022.02
Authors
Han, L.,Zhang, K. (deposition date: 2021-06-08, release date: 2022-05-18, Last modification date: 2022-06-01)
Primary citationHan, L.,Rao, Q.,Yang, R.,Wang, Y.,Chai, P.,Xiong, Y.,Zhang, K.
Cryo-EM structure of an active central apparatus.
Nat.Struct.Mol.Biol., 29:472-482, 2022
Cited by
PubMed Abstract: Accurately regulated ciliary beating in time and space is critical for diverse cellular activities, which impact the survival and development of nearly all eukaryotic species. An essential beating regulator is the conserved central apparatus (CA) of motile cilia, composed of a pair of microtubules (C1 and C2) associated with hundreds of protein subunits per repeating unit. It is largely unclear how the CA plays its regulatory roles in ciliary motility. Here, we present high-resolution structures of Chlamydomonas reinhardtii CA by cryo-electron microscopy (cryo-EM) and its dynamic conformational behavior at multiple scales. The structures show how functionally related projection proteins of CA are clustered onto a spring-shaped scaffold of armadillo-repeat proteins, facilitated by elongated rachis-like proteins. The two halves of the CA are brought together by elastic chain-like bridge proteins to achieve coordinated activities. We captured an array of kinesin-like protein (KLP1) in two different stepping states, which are actively correlated with beating wave propagation of cilia. These findings establish a structural framework for understanding the role of the CA in cilia.
PubMed: 35578022
DOI: 10.1038/s41594-022-00769-9
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon