4v4o

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(Difference between revisions)

Revision as of 13:20, 1 September 2015

Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus

Structural highlights

4v4o is a 42 chain structure with sequence from Thermus thermophilus. This structure supersedes and combines the now removed PDB entries 1we3 and 1wf4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1we3, 1wf4
Resources:	FirstGlance, OCA, RCSB, PDBsum

Warning: this is a large structure, and loading might take a long time or not happen at all.

Function

[CH60_THET2] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).[HAMAP-Rule:MF_00600] [CH10_THET2] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (By similarity).

Publication Abstract from PubMed

The chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein, ATP, and GroES, generating a ternary complex in which protein folding occurs within the cavity capped by GroES (cis-cavity). We determined the crystal structure of the native GroEL-GroES-ADP homolog from Thermus thermophilus, with substrate proteins in the cis-cavity, at 2.8 A resolution. Twenty-four in vivo substrate proteins within the cis-cavity were identified from the crystals. The structure around the cis-cavity, which encapsulates substrate proteins, shows significant differences from that observed for the substrate-free Escherichia coli GroEL-GroES complex. The apical domain around the cis-cavity of the Thermus GroEL-GroES complex exhibits a large deviation from the 7-fold symmetry. As a result, the GroEL-GroES interface differs considerably from the previously reported E. coli GroEL-GroES complex, including a previously unknown contact between GroEL and GroES.

Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.,Shimamura T, Koike-Takeshita A, Yokoyama K, Masui R, Murai N, Yoshida M, Taguchi H, Iwata S Structure. 2004 Aug;12(8):1471-80. PMID:15296740^[1]

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

References

↑ Shimamura T, Koike-Takeshita A, Yokoyama K, Masui R, Murai N, Yoshida M, Taguchi H, Iwata S. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Structure. 2004 Aug;12(8):1471-80. PMID:15296740 doi:10.1016/j.str.2004.05.020

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4v4o"

@@ Line 2: / Line 2: @@
 <StructureSection load='4v4o' size='340' side='right' caption='[[4v4o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4v4o]] is a 42 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. This structure supersedes the now removed PDB entries  and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1wf4 1wf4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V4O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4v4o]] is a 42 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1we3 1we3] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1wf4 1wf4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V4O FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1we3|1we3]], [[1wf4|1wf4]]</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=4v4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v4o RCSB], [http://www.ebi.ac.uk/pdbsum/4v4o PDBsum]</span></td></tr>
 </table>
+{{Large structure}}
 == Function ==
 [[http://www.uniprot.org/uniprot/CH60_THET2 CH60_THET2]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).[HAMAP-Rule:MF_00600] [[http://www.uniprot.org/uniprot/CH10_THET2 CH10_THET2]] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (By similarity).
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+==See Also==
+*[[Chaperonin|Chaperonin]]
 == References ==
 <references/>

4v4o

From Proteopedia

Revision as of 13:20, 1 September 2015

Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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