1we3
From Proteopedia
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|PDB= 1we3 |SIZE=350|CAPTION= <scene name='initialview01'>1we3</scene>, resolution 2.80Å | |PDB= 1we3 |SIZE=350|CAPTION= <scene name='initialview01'>1we3</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1wf4|1WF4]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1we3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1we3 OCA], [http://www.ebi.ac.uk/pdbsum/1we3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1we3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Yokoyama, K.]] | [[Category: Yokoyama, K.]] | ||
[[Category: Yoshida, M.]] | [[Category: Yoshida, M.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: DMS]] | ||
| - | [[Category: MG]] | ||
[[Category: adp]] | [[Category: adp]] | ||
[[Category: atp]] | [[Category: atp]] | ||
| Line 45: | Line 45: | ||
[[Category: hsp60]] | [[Category: hsp60]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:34:59 2008'' |
Revision as of 21:35, 30 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1WF4
| ||||||
| 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
1WE3 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
Page seeded by OCA on Mon Mar 31 00:34:59 2008
Categories: Protein complex | Thermus thermophilus | Iwata, S. | Koike-Takeshita, A. | Masui, R. | Murai, N. | Shimamura, T. | Taguchi, H. | Yokoyama, K. | Yoshida, M. | Adp | Atp | Chaperone | Chaperonin | Cpn10 | Cpn60 | Folding | Groel | Roe | Hsp10 | Hsp60
