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9GOS

CryoEM structure of the native Chlamydomonas reinhardtii Flagella Membrane Glycoprotein 1B.

Summary for 9GOS
Entry DOI10.2210/pdb9gos/pdb
EMDB information51499
DescriptorFlagella Membrane Glycoprotein 1B (1 entity in total)
Functional Keywordsmucin, glycoprotein, glycocalyx, membrane protein
Biological sourceChlamydomonas reinhardtii
Total number of polymer chains1
Total formula weight448226.63
Authors
Nievergelt, A.P.,Hoepfner, L.M.,Matrino, F.,Scholz, M.,Foster, H.E.,Rodenfels, J.,von Appen, A.,Hippler, M.,Pigino, G. (deposition date: 2024-09-06, release date: 2025-05-07, Last modification date: 2025-11-19)
Primary citationHoepfner, L.M.,Nievergelt, A.P.,Matrino, F.,Scholz, M.,Foster, H.E.,Rodenfels, J.,von Appen, A.,Hippler, M.,Pigino, G.
Unwrapping the Ciliary Coat: High-Resolution Structure and Function of the Ciliary Glycocalyx.
Adv Sci, 12:e2413355-e2413355, 2025
Cited by
PubMed Abstract: The glycocalyx, a highly heterogeneous glycoprotein layer of cilia regulates adhesion and force transduction and is involved in signaling. The high-resolution molecular architecture of this layer is currently not understood. The structure of the ciliary coat is described in the green alga Chlamydomonas reinhardtii by cryo-electron tomography and proteomic approaches and the high-resolution cryoEM structure of the main component, FMG1B is solved. FMG1B is described as a mucin orthologue which lacks the major O-glycosylation of mammalian mucins but is N-glycosylated. FMG1A, a previously undescribed isoform of FMG1B is expressed in C. reinhardtii. By microflow-based adhesion assays, increased surface adhesion in the glycocalyx deficient double-mutant fmg1b-fmg1a is observed. It is found this mutant is capable of surface-gliding, with neither isoform required for extracellular force transduction by intraflagellar transport. The results find FMG1 to form a protective layer with adhesion-regulative instead of adhesion-conferring properties and an example of an undescribed class of mucins.
PubMed: 40041987
DOI: 10.1002/advs.202413355
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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