Motor Mechanism for Protein Threading through Hsp104
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چکیده
منابع مشابه
Motor Mechanism for Protein Threading through Hsp104
The protein-remodeling machine Hsp104 dissolves amorphous aggregates as well as ordered amyloid assemblies such as yeast prions. Force generation originates from a tandem AAA+ (ATPases associated with various cellular activities) cassette, but the mechanism and allostery of this action remain to be established. Our cryoelectron microscopy maps of Hsp104 hexamers reveal substantial domain moveme...
متن کاملEvidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.
Saccharomyces cerevisiae Hsp104, a hexameric member of the Hsp100/Clp subfamily of AAA+ ATPases with two nucleotide binding domains (NBD1 and 2), refolds aggregated proteins in conjunction with Hsp70 molecular chaperones. Hsp104 may act as a "molecular crowbar" to pry aggregates apart and/or may extract proteins from aggregates by unfolding and threading them through the axial channel of the Hs...
متن کاملProtein Threading
The most important in silico methods, to exploit the amount of new genomic data, are based on the concept of homology. The principle of homology-based analysis is to identify a homology relationship between a new protein and a protein whose function is known. For remote homologs, sequence alignment methods fail. In such a case one aligns the sequence of a new protein with the 3D structures of k...
متن کاملGenetic Algorithms for Protein Threading
Despite many years of efforts, a direct prediction of protein structure from sequence is still not possible. As a result, in the last few years researchers have started to address the "inverse folding problem": Identifying and aligning a sequence to the fold with which it is most compatible, a process known as "threading". In two meetings in which protein folding predictions were objectively ev...
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By using techniques borrowed from statistical physics and neural networks, we determine the parameters, associated with a scoring function, that are chosen optimally to ensure complete success in threading tests in a training set of proteins. These parameters provide a quantitative measure of the propensities of amino acids to be buried or exposed and to be in a given secondary structure and ar...
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ژورنال
عنوان ژورنال: Molecular Cell
سال: 2009
ISSN: 1097-2765
DOI: 10.1016/j.molcel.2009.02.026