GroEL-GroES Cycling
نویسندگان
چکیده
منابع مشابه
GroEL-GroES-mediated protein folding.
The chaperonin-mediated folding reaction is an essential ATP-dependent reaction that provides kinetic assistance to the process of protein folding to the native state in a variety of cellular compartments. This reaction, carried out by a megadalton-sized double ring “machine,” remains a fascination because it exhibits a multitude of interesting features, for example, allostery, with both positi...
متن کاملMolecular mechanisms of chaperonin GroEL-GroES function.
The dynamics of the GroEL-GroES complex is investigated with a coarse-grained model. This model is one in which single-residue points are connected to other such points, which are nearby, by identical springs, forming a network of interactions. The nature of the most important (slowest) normal modes reveals a wide variety of motions uniquely dependent upon the central cavity of the structure, i...
متن کاملGroEL-GroES Cycling ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings
The double-ring chaperonin GroEL mediates protein folding in the central cavity of a ring bound by ATP and GroES, but it is unclear how GroEL cycles from one folding-active complex to the next. We observe that hydrolysis of ATP within the cis ring must occur before either nonnative polypeptide or GroES can bind to the trans ring, and this is associated with reorientation of the trans ring apica...
متن کاملProtein unfolding and folding by GroEL-GroES
Background: Chaperonins like the GroEL-GroES complex facilitate protein folding in the cell. Results: Substrate proteins are captured by the open, trans ring of the GroEL-ATP-GroES complex and are partially unfolded. Conclusion: Maximally efficient folding requires repeated cycles of substrate protein unfolding by the GroEL-GroES complex. Significance: Establishing how substrate proteins are pr...
متن کاملGroEL-GroES-mediated protein folding requires an intact central cavity.
The chaperonin GroEL is an oligomeric double ring structure that, together with the cochaperonin GroES, assists protein folding. Biochemical analyses indicate that folding occurs in a cis ternary complex in which substrate is sequestered within the GroEL central cavity underneath GroES. Recently, however, studies of GroEL "minichaperones" containing only the apical substrate binding subdomain h...
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ژورنال
عنوان ژورنال: Cell
سال: 1999
ISSN: 0092-8674
DOI: 10.1016/s0092-8674(00)80742-4