Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin11Edited by W. Baumeister

2002 ◽  
Vol 315 (1) ◽  
pp. 73-85 ◽  
Author(s):  
Takao Yoshida ◽  
Rika Kawaguchi ◽  
Hideki Taguchi ◽  
Masasuke Yoshida ◽  
Takuo Yasunaga ◽  
...  
Keyword(s):  
Protein Folding ◽  
Group Ii ◽  
Group Ii Chaperonin

scholarly journals Structural analysis of the Sulfolobus solfataricus TF55β chaperonin by cryo-electron microscopy

2021 ◽  
Vol 77 (3) ◽  
pp. 79-84
Author(s):  
Yi Cheng Zeng ◽  
Meghna Sobti ◽  
Alastair G. Stewart
Keyword(s):  
Electron Microscopy ◽  
Protein Folding ◽  
Structural Analysis ◽  
Sulfolobus Solfataricus ◽  
Nucleotide Exchange ◽  
Cryo Electron Microscopy ◽  
Biomolecular Complexes ◽  
Group Ii ◽  
Group Ii Chaperonin ◽  
Archaeal Genus

Chaperonins are biomolecular complexes that assist in protein folding. Thermophilic factor 55 (TF55) is a group II chaperonin found in the archaeal genus Sulfolobus that has α, β and γ subunits. Using cryo-electron microscopy, structures of the β-only complex of S. solfataricus TF55 (TF55β) were determined to 3.6–4.2 Å resolution. The structures of the TF55β complexes formed in the presence of ADP or ATP highlighted an open state in which nucleotide exchange can occur before progressing in the refolding cycle.

scholarly journals Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle

2010 ◽  
Vol 285 (36) ◽  
pp. 27958-27966 ◽  
Author(s):  
Jose H. Pereira ◽  
Corie Y. Ralston ◽  
Nicholai R. Douglas ◽  
Daniel Meyer ◽  
Kelly M. Knee ◽  
...  
Keyword(s):  
Protein Folding ◽  
Crystal Structures ◽  
Group Ii ◽  
Group Ii Chaperonin

Glycine at the 65th Position Plays an Essential Role in ATP-Dependent Protein Folding by Archael Group II Chaperonin

2001 ◽  
Vol 289 (5) ◽  
pp. 1118-1124 ◽  
Author(s):  
Ryo Iizuka ◽  
Takao Yoshida ◽  
Tadashi Maruyama ◽  
Yasuhito Shomura ◽  
Kunio Miki ◽  
...  
Keyword(s):  
Protein Folding ◽  
Essential Role ◽  
Dependent Protein ◽  
Group Ii ◽  
Group Ii Chaperonin

Purification and Molecular Cloning of the Group II Chaperonin from the Acidothermophilic Archaeon,SulfolobusSp. Strain 7

1997 ◽  
Vol 236 (3) ◽  
pp. 727-732 ◽  
Author(s):  
Norihiro Nakamura ◽  
Hideki Taguchi ◽  
Noriyuki Ishii ◽  
Masasuke Yoshida ◽  
Makoto Suzuki ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Group Ii ◽  
Group Ii Chaperonin

scholarly journals Role of the Helical Protrusion in the Conformational Change and Molecular Chaperone Activity of the Archaeal Group II Chaperonin

2004 ◽  
Vol 279 (18) ◽  
pp. 18834-18839 ◽  
Author(s):  
Ryo Iizuka ◽  
Sena So ◽  
Tomonao Inobe ◽  
Takao Yoshida ◽  
Tamotsu Zako ◽  
...  
Keyword(s):  
Conformational Change ◽  
Molecular Chaperone ◽  
Chaperone Activity ◽  
Group Ii ◽  
Group Ii Chaperonin

scholarly journals Expression, purification, crystallization and X-ray diffraction studies of the molecular chaperone prefoldin fromHomo sapiens

2015 ◽  
Vol 71 (9) ◽  
pp. 1189-1193 ◽  
Author(s):  
Yoshiki Aikawa ◽  
Hiroshi Kida ◽  
Yuichi Nishitani ◽  
Kunio Miki
Keyword(s):  
Crystal Structure ◽  
Protein Folding ◽  
Diffraction Data ◽  
Molecular Chaperone ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Native Proteins ◽  
Group Ii Chaperonin

Proper protein folding is an essential process for all organisms. Prefoldin (PFD) is a molecular chaperone that assists protein folding by delivering non-native proteins to group II chaperonin. A heterohexamer of eukaryotic PFD has been shown to specifically recognize and deliver non-native actin and tubulin to chaperonin-containing TCP-1 (CCT), but the mechanism of specific recognition is still unclear. To determine its crystal structure, recombinant human PFD was reconstituted, purified and crystallized. X-ray diffraction data were collected to 4.7 Å resolution. The crystals belonged to space groupP21212, with unit-cell parametersa= 123.2,b= 152.4,c= 105.9 Å.

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