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1wf4

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|PDB= 1wf4 |SIZE=350|CAPTION= <scene name='initialview01'>1wf4</scene>, resolution 2.80&Aring;
|PDB= 1wf4 |SIZE=350|CAPTION= <scene name='initialview01'>1wf4</scene>, resolution 2.80&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=DMS:DIMETHYL SULFOXIDE'>DMS</scene>
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1we3|1WE3]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wf4 OCA], [http://www.ebi.ac.uk/pdbsum/1wf4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wf4 RCSB]</span>
}}
}}
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[[Category: Yokoyama, K.]]
[[Category: Yokoyama, K.]]
[[Category: Yoshida, M.]]
[[Category: Yoshida, M.]]
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[[Category: ADP]]
 
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[[Category: DMS]]
 
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[[Category: MG]]
 
[[Category: adp]]
[[Category: adp]]
[[Category: atp]]
[[Category: atp]]
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[[Category: hsp60]]
[[Category: hsp60]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:06:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:35:23 2008''

Revision as of 21:35, 30 March 2008

Image:1wf4.gif


PDB ID 1wf4

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands: , ,
Related: 1WE3


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1WF4 is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

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

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