4a13 | pdb_00004a13
From Proteopedia
model refined against symmetry-free cryo-EM map of TRiC-ADP
Template:ABSTRACT PUBMED 22045336
Function
[TCPB_BOVIN] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
About this Structure
4a13 is a 16 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
- Cong Y, Schroder GF, Meyer AS, Jakana J, Ma B, Dougherty MT, Schmid MF, Reissmann S, Levitt M, Ludtke SL, Frydman J, Chiu W. Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle. EMBO J. 2011 Nov 1;31(3):720-30. doi: 10.1038/emboj.2011.366. PMID:22045336 doi:10.1038/emboj.2011.366
