Inter-ring communication allows the GroEL chaperonin complex to distinguish between different substrates
نویسندگان
چکیده
منابع مشابه
Identi®cation of in vivo substrates of the chaperonin GroEL
* Department of Cellular Biochemistry, 2 GSF-Forschungszentrum fuÈr Umwelt und Gesundheit, Munich Information Center for Protein Sequences, and § Department of Protein Analytics, Max-Planck-Institut fuÈr Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany 3 Toplab GmbH, Proteomics Division, Fraunhoferstrasse 18A, D-82152 Martinsried, Germany ...............................................
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The chaperonin GroEL consists of a double-ring structure made of identical subunits and displays unusual allosteric properties caused by the interaction between its constituent subunits. Cooperative binding of ATP to a protein ring allows binding of GroES to that ring, and at the same time negative inter-ring cooperativity discharges the ligands from the opposite ring, thus driving the protein-...
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The chaperonin GroEL consists of a double-ring structure that assists protein folding in the presence of GroES and ATP. Recent studies suggest that the 7-mer ring is the functional unit where protein folding takes place. Nevertheless, both GroEL rings are required to complete the reaction cycle through signals transmitted between the two rings. Electron microscopy, image processing, and biochem...
متن کاملThe inter-ring arrangement of the cytosolic chaperonin CCT.
The eukaryotic cytosolic chaperonin CCT (chaperonin containing TCP-1) is the most complex of all chaperonins-an oligomeric structure built from two identical rings, each composed of single copies of eight different subunits. The arrangement of the eight subunits within each ring has been characterised for some time, but the phasing between the two rings remains unknown. Here, three-dimensional ...
متن کاملStructure and allostery of the chaperonin GroEL.
Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of subunits presenting end cavities lined with hydrophobic binding sites for nonnative polypeptides. Once bound, substrates are subjected to forceful, concerted movements that result in their ejection from the binding surface and simultaneous encapsulation inside a hydrophilic chamber that favors their foldi...
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ژورنال
عنوان ژورنال: Protein Science
سال: 2007
ISSN: 0961-8368,1469-896X
DOI: 10.1110/ps.062713607