Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 426, Issue 21, Pages 3634-3641Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2014.08.017
Keywords
folding; chaperone; chaperonin; nanomachine; inter-ring contacts
Categories
Funding
- SPring-8 [2011B1136, 2012A1472, 2013A1379, 2013B1184]
- Japan Society for the Promotion of Science [20870035, 24370044, 26102725, 19058002, 17049009]
- Ministry of Education, Culture, Sports, Science and Technology, Japan
- Takeda Science Foundation
- Uehara Memorial Foundation
- National Project on Protein Structural and Functional Analyses from Ministry of Education, Culture, Sports, Science and Technology
- Research Acceleration Program of Japan Science and Technology Agency
- Grants-in-Aid for Scientific Research [17049009, 20870035, 26102725, 25440055] Funding Source: KAKEN
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The chaperonin GroEL is an essential chaperone that assists in protein folding with the aid of GroES and ATP. GroEL forms a double-ring structure, and both rings can bind GroES in the presence of ATP. Recent progress on the GroEL mechanism has revealed the importance of a symmetric 1:2 GroEL:GroES(2) complex (the football-shaped complex) as a critical intermediate during the functional GroEL cycle. We determined the crystal structure of the football GroEL:GroES(2)-ATP(14) complex from Escherichia coli at 3.8 angstrom, using a GroEL mutant that is extremely defective in ATP hydrolysis. The overall structure of the football complex resembled the GroES-bound GroEL ring of the asymmetric 1:1 GroEL:GroES complex (the bullet complex). However, the two GroES-bound GroEL rings form a modified interface by an similar to 7 degrees rotation about the 7-fold axis. As a result, the inter-ring contacts between the two GroEL rings in the football complex differed from those in the bullet complex. The differences provide a structural basis for the apparently impaired inter-ring negative cooperativity observed in several biochemical analyses. (C) 2014 Elsevier Ltd. All rights reserved.
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