This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4v4o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "4v4o" [edit=sysop:move=sysop])
Current revision (09:01, 20 March 2024) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus==
==Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus==
-
<StructureSection load='4v4o' size='340' side='right' caption='[[4v4o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+
<StructureSection load='4v4o' size='340' side='right'caption='[[4v4o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== 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 [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. This structure supersedes 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 [https://proteopedia.org/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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4v4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4o OCA], [https://pdbe.org/4v4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4o RCSB], [https://www.ebi.ac.uk/pdbsum/4v4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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).
+
[https://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]
-
<div style="background-color:#fffaf0;">
+
-
== 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<ref>PMID:15296740</ref>
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
==See Also==
-
</div>
+
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
-
[[Category: Iwata, S]]
+
[[Category: Iwata S]]
-
[[Category: Koike-Takeshita, A]]
+
[[Category: Koike-Takeshita A]]
-
[[Category: Masui, R]]
+
[[Category: Masui R]]
-
[[Category: Murai, N]]
+
[[Category: Murai N]]
-
[[Category: Shimamura, T]]
+
[[Category: Shimamura T]]
-
[[Category: Taguchi, H]]
+
[[Category: Taguchi H]]
-
[[Category: Yokoyama, K]]
+
[[Category: Yokoyama K]]
-
[[Category: Yoshida, M]]
+
[[Category: Yoshida M]]
-
[[Category: Adp]]
+
-
[[Category: Atp]]
+
-
[[Category: Chaperone]]
+
-
[[Category: Chaperonin]]
+
-
[[Category: Cpn10]]
+
-
[[Category: Cpn60]]
+
-
[[Category: Folding]]
+
-
[[Category: Groel]]
+
-
[[Category: Roe]]
+
-
[[Category: Hsp10]]
+
-
[[Category: Hsp60]]
+

Current revision

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

PDB ID 4v4o

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools