4b2t

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4b2t]] is a 16 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4B2T FirstGlance]. <br>
<table><tr><td colspan='2'>[[4b2t]] is a 16 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4B2T FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xsm|2xsm]], [[4aol|4aol]], [[4apk|4apk]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 5.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2t OCA], [https://pdbe.org/4b2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b2t RCSB], [https://www.ebi.ac.uk/pdbsum/4b2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b2t ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2t OCA], [https://pdbe.org/4b2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b2t RCSB], [https://www.ebi.ac.uk/pdbsum/4b2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b2t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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). [[https://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). [[https://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). [[https://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). [[https://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). [[https://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). [[https://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).
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[https://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).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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.
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In eukaryotes, CCT is essential for the correct and efficient folding of many cytosolic proteins, most notably actin and tubulin. Structural studies of CCT have been hindered by the failure of standard crystallographic analysis to resolve its eight different subunit types at low resolutions. Here, we exhaustively assess the R value fit of all possible CCT models to available crystallographic data of the closed and open forms with resolutions of 3.8 A and 5.5 A, respectively. This unbiased analysis finds the native subunit arrangements with overwhelming significance. The resulting structures provide independent crystallographic proof of the subunit arrangement of CCT and map major asymmetrical features of the particle onto specific subunits. The actin and tubulin substrates both bind around subunit CCT6, which shows other structural anomalies. CCT is thus clearly partitioned, both functionally and evolutionary, into a substrate-binding side that is opposite to the ATP-hydrolyzing side.
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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>
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The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional Partitioning.,Kalisman N, Schroder GF, Levitt M Structure. 2013 Mar 5. pii: S0969-2126(13)00039-7. doi:, 10.1016/j.str.2013.01.017. PMID:23478063<ref>PMID:23478063</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kalisman, N]]
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[[Category: Kalisman N]]
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[[Category: Levitt, M]]
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[[Category: Levitt M]]
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[[Category: Schroeder, G F]]
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[[Category: Schroeder GF]]
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[[Category: Chaperone]]
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Current revision

The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning

PDB ID 4b2t

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