Cryo-EM structure of a 16.5-kDa small heat-shock protein from Methanocaldococcus jannaschii
Author:
Funder
Ministry of Science, ICT and Future Planning
Korea Basic Science Institute
National Research Foundation of Korea
Publisher
Elsevier BV
Subject
Molecular Biology,General Medicine,Biochemistry,Structural Biology
Reference57 articles.
1. Transcriptional profiling of the hyperthermophilic methanarchaeon Methanococcus jannaschii in response to lethal heat and non-lethal cold shock;Boonyaratanakornkit;Environ. Microbiol.,2005
2. Transcriptional responses of the deep-sea hyperthermophile Methanocaldococcus jannaschii under shifting extremes of temperature and pressure;Boonyaratanakornkit;Extremophiles,2007
3. Activation mechanism of HSP16.5 from Methanococcus jannaschii;Kim;Biochem. Biophys. Res. Commun.,2003
4. Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107G, in the alpha-crystallin domain;Quinlan;Philos. Trans. R. Soc. Lond. B Biol. Sci.,2013
5. Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding;Shi;J. Biol. Chem.,2013
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