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5gw5

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Revision as of 20:08, 10 April 2020

Structure of TRiC-AMP-PNP

5gw5, resolution 4.60Å

Structural highlights

5gw5 is a 16 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5gw4
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TCPH_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [TCPD_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [TCPQ_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity). [TCPB_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [TCPZ_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [TCPA_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [TCPE_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. [TCPG_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.

Publication Abstract from PubMed

The eukaryotic chaperonin TRiC (or CCT) assists in the folding of 10% of cytosolic proteins. Here we present two cryo-EM structures of Saccharomyces cerevisiae TRiC in a newly identified nucleotide partially preloaded (NPP) state and in the ATP-bound state, at 4.7-A and 4.6-A resolution, respectively. Through inner-subunit eGFP tagging, we identified the subunit locations in open-state TRiC and found that the CCT2 subunit pair forms an unexpected Z shape. ATP binding induces a dramatic conformational change on the CCT2 side, thereby suggesting that CCT2 plays an essential role in TRiC allosteric cooperativity. Our structural and biochemical data reveal a staggered ATP binding mechanism of TRiC with preloaded nucleotide on the CCT6 side of NPP-TRiC and demonstrate that TRiC has evolved into a complex that is structurally divided into two sides. This work offers insight into how the TRiC nucleotide cycle coordinates with its mechanical cycle in preparing folding intermediates for further productive folding.

Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.,Zang Y, Jin M, Wang H, Cui Z, Kong L, Liu C, Cong Y Nat Struct Mol Biol. 2016 Dec;23(12):1083-1091. doi: 10.1038/nsmb.3309. Epub 2016, Oct 24. PMID:27775711^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zang Y, Jin M, Wang H, Cui Z, Kong L, Liu C, Cong Y. Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM. Nat Struct Mol Biol. 2016 Dec;23(12):1083-1091. doi: 10.1038/nsmb.3309. Epub 2016, Oct 24. PMID:27775711 doi:http://dx.doi.org/10.1038/nsmb.3309

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5gw5"

@@ Line 3: / Line 3: @@
 <SX load='5gw5' size='340' side='right' viewer='molstar' caption='[[5gw5]], [[Resolution|resolution]] 4.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5gw5]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GW5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5gw5]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GW5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GW5 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gw4|5gw4]]</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=5gw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gw5 OCA], [http://pdbe.org/5gw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gw5 RCSB], [http://www.ebi.ac.uk/pdbsum/5gw5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gw5 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gw5 OCA], [http://pdbe.org/5gw5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gw5 RCSB], [http://www.ebi.ac.uk/pdbsum/5gw5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gw5 ProSAT]</span></td></tr>
 </table>
 == Function ==

5gw5

From Proteopedia

Revision as of 20:08, 10 April 2020

Structure of TRiC-AMP-PNP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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