Function of a thermophilic archaeal chaperonin is enhanced by electrostatic interactions with its targets
Author:
Funder
Japan Society for the Promotion of Science (JSPS)
Kwansei Gakuin University
Publisher
Elsevier BV
Subject
Applied Microbiology and Biotechnology,Bioengineering,Biotechnology
Reference22 articles.
1. Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei;Hirtreiter;Mol. Microbiol.,2009
2. Indole-3-glycerol-phosphate synthase is recognized by a cold-inducible group II chaperonin in Thermococcus kodakarensis;Gao;Appl. Environ. Microbiol.,2012
3. Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins;Spiess;Mol. Cell,2006
4. The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT;Joachimiak;Cell,2014
5. Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms;Shomura;J. Mol. Biol.,2004
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