4b2t
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning== | |
| - | + | <StructureSection load='4b2t' size='340' side='right' caption='[[4b2t]], [[Resolution|resolution]] 5.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4b2t]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B2T FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xsm|2xsm]], [[4aol|4aol]], [[4apk|4apk]]</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b2t RCSB], [http://www.ebi.ac.uk/pdbsum/4b2t PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/TCPH_BOVIN TCPH_BOVIN]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). [[http://www.uniprot.org/uniprot/TCPD_BOVIN TCPD_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). [[http://www.uniprot.org/uniprot/TCPQ_BOVIN TCPQ_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). [[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). [[http://www.uniprot.org/uniprot/TCPZ_BOVIN TCPZ_BOVIN]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). [[http://www.uniprot.org/uniprot/TCPA_BOVIN TCPA_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). [[http://www.uniprot.org/uniprot/TCPG_BOVIN TCPG_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). | [[http://www.uniprot.org/uniprot/TCPH_BOVIN TCPH_BOVIN]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). [[http://www.uniprot.org/uniprot/TCPD_BOVIN TCPD_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). [[http://www.uniprot.org/uniprot/TCPQ_BOVIN TCPQ_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). [[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). [[http://www.uniprot.org/uniprot/TCPZ_BOVIN TCPZ_BOVIN]] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). [[http://www.uniprot.org/uniprot/TCPA_BOVIN TCPA_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). [[http://www.uniprot.org/uniprot/TCPG_BOVIN TCPG_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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein folding is assisted by molecular chaperones. CCT (chaperonin containing TCP-1, or TRiC) is a 1-MDa oligomer that is built by two rings comprising eight different 60-kDa subunits. This chaperonin regulates the folding of important proteins including actin, alpha-tubulin and beta-tubulin. We used an electron density map at 5.5 A resolution to reconstruct CCT, which showed a substrate in the inner cavities of both rings. Here we present the crystal structure of the open conformation of this nanomachine in complex with tubulin, providing information about the mechanism by which it aids tubulin folding. The structure showed that the substrate interacts with loops in the apical and equatorial domains of CCT. The organization of the ATP-binding pockets suggests that the substrate is stretched inside the cavity. Our data provide the basis for understanding the function of this chaperonin. | ||
| + | |||
| + | Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin.,Munoz IG, Yebenes H, Zhou M, Mesa P, Serna M, Park AY, Bragado-Nilsson E, Beloso A, de Carcer G, Malumbres M, Robinson CV, Valpuesta JM, Montoya G Nat Struct Mol Biol. 2010 Dec 12. PMID:21151115<ref>PMID:21151115</ref> | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Chaperonin|Chaperonin]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Kalisman, N | + | [[Category: Kalisman, N]] |
| - | [[Category: Levitt, M | + | [[Category: Levitt, M]] |
| - | [[Category: Schroeder, G F | + | [[Category: Schroeder, G F]] |
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
Revision as of 04:10, 25 December 2014
The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning
| |||||||||||
