Crystal Structure of the Native Chaperonin Complex from Thermus thermophilus Revealed Unexpected Asymmetry at the cis-Cavity-Reference-Cited by-同舟云学术

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Crystal Structure of the Native Chaperonin Complex from Thermus thermophilus Revealed Unexpected Asymmetry at the cis-Cavity

Published:2004-08 Issue:8 Volume:12 Page:1471-1480
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Shimamura Tatsuro,Koike-Takeshita Ayumi,Yokoyama Ken,Masui Ryoji,Murai Noriyuki,Yoshida Masasuke,Taguchi Hideki,Iwata So

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference52 articles.

1. GroEL binds artificial proteins with random sequences;Aoki;J. Biol. Chem.,2000

2. Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospray ionization mass spectrometry and fluorescence binding studies;Ashcroft;J. Biol. Chem.,2002

3. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å;Braig;Nature,1994

4. Conformational variability in the refined structure of the chaperonin GroEL at 2.8Å resolution;Braig;Nat. Struct. Biol.,1995

5. Dual function of protein confinement in chaperonin-assisted protein folding;Brinker;Cell,2001

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