Mechanism of folding chamber closure in a group II chaperonin

Nature

Volumn 463, Issue 7279, 2010, Pages 379-383

  Zhang, Junjie ^a,b   Baker, Matthew L ^b   Schröder, Gunnar F ^c,e   Douglas, Nicholai R ^d   Reissmann, Stefanie ^d,f   Jakana, Joanita ^b   Dougherty, Matthew ^b   Fu, Caroline J ^b   Levitt, Michael ^c   Ludtke, Steven J ^a,b   Frydman, Judith ^d   Chiu, Wah ^a,b  

^a Graduate Program in Structural and Computational Biology and Molecular Biophysics   (United States)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

^c Department of Structural Biology ^*

^d STANFORD UNIVERSITY   (United States)

^e FORSCHUNGSZENTRUM JÜLICH   (Germany)

^f MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL PROTEIN; CHAPERONIN; NUCLEOTIDE;

ELECTRON MICROSCOPY; EUKARYOTE; GENETIC ANALYSIS; HYDROLYSIS; PEPTIDE; PROKARYOTE;

ALLOSTERISM; ARTICLE; CRYOELECTRON MICROSCOPY; HYDROLYSIS; MACROMOLECULE; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

ADENOSINE TRIPHOSPHATE; ALLOSTERIC REGULATION; BINDING SITES; CRYOELECTRON MICROSCOPY; GROUP II CHAPERONINS; HYDROLYSIS; METHANOCOCCUS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SUBUNITS; STRUCTURE-ACTIVITY RELATIONSHIP;

ARCHAEA; EUKARYOTA;

EID: 75149145980     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08701     Document Type: Article

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