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| [[Image:1we3.jpg|left|200px]] | | #REDIRECT [[4v4o]] This PDB entry is obsolete and replaced by 4v4o |
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| {{Structure
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| |PDB= 1we3 |SIZE=350|CAPTION= <scene name='initialview01'>1we3</scene>, resolution 2.80Å
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| |SITE=
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| |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>
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| |ACTIVITY=
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| |GENE=
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| |DOMAIN=
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| |RELATEDENTRY=[[1wf4|1WF4]]
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| |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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| }}
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| '''Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus'''
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| ==Overview==
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| 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.
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| ==About this Structure==
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| 1WE3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WE3 OCA].
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| ==Reference==
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| 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:[http://www.ncbi.nlm.nih.gov/pubmed/15296740 15296740]
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| [[Category: Protein complex]]
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| [[Category: Thermus thermophilus]]
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| [[Category: Iwata, S.]]
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| [[Category: Koike-Takeshita, A.]]
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| [[Category: Masui, R.]]
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| [[Category: Murai, N.]]
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| [[Category: Shimamura, T.]]
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| [[Category: Taguchi, H.]]
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| [[Category: Yokoyama, K.]]
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| [[Category: Yoshida, M.]]
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| [[Category: adp]]
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| [[Category: atp]]
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| [[Category: chaperone]]
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| [[Category: chaperonin]]
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| [[Category: cpn10]]
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| [[Category: cpn60]]
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| [[Category: folding]]
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| [[Category: groel]]
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| [[Category: roe]]
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| [[Category: hsp10]]
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| [[Category: hsp60]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:34:59 2008''
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