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5UCY

Cryo-EM map of protofilament of microtubule doublet

Summary for 5UCY
Entry DOI10.2210/pdb5ucy/pdb
Related5UBQ
EMDB information8528 8532 8537 8539
DescriptorTubulin alpha chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
Functional Keywordscilia, doublet, protofilament, tubulin, structural protein
Biological sourceTetrahymena thermophila
More
Total number of polymer chains2
Total formula weight97788.14
Authors
Ichikawa, M.,Liu, D.,Kastritis, P.L.,Basu, K.,Bui, K.H. (deposition date: 2016-12-22, release date: 2017-05-10, Last modification date: 2020-01-15)
Primary citationIchikawa, M.,Liu, D.,Kastritis, P.L.,Basu, K.,Hsu, T.C.,Yang, S.,Bui, K.H.
Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins.
Nat Commun, 8:15035-15035, 2017
Cited by
PubMed Abstract: Cilia are ubiquitous, hair-like appendages found in eukaryotic cells that carry out functions of cell motility and sensory reception. Cilia contain an intriguing cytoskeletal structure, termed the axoneme that consists of nine doublet microtubules radially interlinked and longitudinally organized in multiple specific repeat units. Little is known, however, about how the axoneme allows cilia to be both actively bendable and sturdy or how it is assembled. To answer these questions, we used cryo-electron microscopy to structurally analyse several of the repeating units of the doublet at sub-nanometre resolution. This structural detail enables us to unambiguously assign α- and β-tubulins in the doublet microtubule lattice. Our study demonstrates the existence of an inner sheath composed of different kinds of microtubule inner proteins inside the doublet that likely stabilizes the structure and facilitates the specific building of the B-tubule.
PubMed: 28462916
DOI: 10.1038/ncomms15035
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.6 Å)
Structure validation

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