4a13
From Proteopedia
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{{STRUCTURE_4a13| PDB=4a13 | SCENE= }} | {{STRUCTURE_4a13| PDB=4a13 | SCENE= }} | ||
| + | ===model refined against symmetry-free cryo-EM map of TRiC-ADP=== | ||
| + | {{ABSTRACT_PUBMED_22045336}} | ||
| - | == | + | ==Function== |
| - | + | [[http://www.uniprot.org/uniprot/TCPB_BOVIN 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). | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:022045336</ref><references group="xtra"/> | + | <ref group="xtra">PMID:022045336</ref><references group="xtra"/><references/> |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Chiu, W.]] | [[Category: Chiu, W.]] | ||
Revision as of 16:28, 19 June 2013
Contents |
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
Categories: Bos taurus | Chiu, W. | Cong, Y. | Dougherty, M T. | Frydman, J. | Jakana, J. | Levitt, M. | Ludtke, S L. | Ma, B. | Meyer, A S. | Reissmann, S. | Schmid, M F. | Schroder, G F. | Chaperone | Chaperonin | Protein folding
