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10.1016/j.jmb.2015.11.016 http://scihub22266oqcxt.onion/10.1016/j.jmb.2015.11.016 C4860052!4860052!26608812     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Biol 2016 ; 428 (9 Pt B): 1870-85 Nephropedia Template TP {{tp|p=26608812|t=2016. Mechanistic and structural insights into the prion-disaggregase activity of Hsp104 |pdf=|usr=}}{{26608812}} gab.com Text Mechanistic and structural insights into the prion-disaggregase activity of Hsp104 JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26608812 #FOAvip Hsp104 is a dynamic ring-translocase and hexameric AAA+ protein found in yeast, which couples ATP hydrolysis to disassembly and reactivation of proteins trapped in soluble preamyloid oligomers, disordered protein aggregates, and stable amyloid or prion conformers. Here, we highlight advances in our structural understanding of Hsp104 and how Hsp104 deconstructs Sup35 prions. Although the atomic structure of Hsp104 hexamers remains uncertain, volumetric reconstruction of Hsp104 hexamers in ATP?S, ADP-AlFx (ATP hydrolysis transition state mimic), and ADP via small-angle x-ray scattering has revealed a peristaltic pumping motion upon ATP hydrolysis. This pumping motion likely drives directional substrate translocation across the central Hsp104 channel. Hsp104 initially engages Sup35 prions immediately C-terminal to their cross-? structure. Directional pulling by Hsp104 then resolves N-terminal cross-? structure in a stepwise manner. First, Hsp104 fragments the prion. Second, Hsp104 unfolds cross-? structure. Third, Hsp104 releases soluble Sup35. Deletion of the Hsp104 N-terminal domain (NTD) yields a hypomorphic disaggregase, Hsp104?N, with an altered pumping mechanism. Hsp104?N fragments Sup35 prions without unfolding cross-? structure or releasing soluble Sup35. Moreover, Hsp104?N activity cannot be enhanced by mutations in the middle domain that potentiate disaggregase activity. Thus, the NTD is critical for the full repertoire of Hsp104 activities. Twit Text FOAVip Mechanistic and structural insights into the prion-disaggregase activity of Hsp104 ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26608812 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26608812 #FOAvip English Wikipedia <ref>{{Cite pmid|26608812}}</ref> Mechanistic and structural insights into the prion-disaggregase activity of Hsp104 #MMPMID26608812 Sweeny EA; Shorter J J Mol Biol 2016[May]; 428 (9 Pt B): 1870-85 PMID26608812show ga Hsp104 is a dynamic ring-translocase and hexameric AAA+ protein found in yeast, which couples ATP hydrolysis to disassembly and reactivation of proteins trapped in soluble preamyloid oligomers, disordered protein aggregates, and stable amyloid or prion conformers. Here, we highlight advances in our structural understanding of Hsp104 and how Hsp104 deconstructs Sup35 prions. Although the atomic structure of Hsp104 hexamers remains uncertain, volumetric reconstruction of Hsp104 hexamers in ATP?S, ADP-AlFx (ATP hydrolysis transition state mimic), and ADP via small-angle x-ray scattering has revealed a peristaltic pumping motion upon ATP hydrolysis. This pumping motion likely drives directional substrate translocation across the central Hsp104 channel. Hsp104 initially engages Sup35 prions immediately C-terminal to their cross-? structure. Directional pulling by Hsp104 then resolves N-terminal cross-? structure in a stepwise manner. First, Hsp104 fragments the prion. Second, Hsp104 unfolds cross-? structure. Third, Hsp104 releases soluble Sup35. Deletion of the Hsp104 N-terminal domain (NTD) yields a hypomorphic disaggregase, Hsp104?N, with an altered pumping mechanism. Hsp104?N fragments Sup35 prions without unfolding cross-? structure or releasing soluble Sup35. Moreover, Hsp104?N activity cannot be enhanced by mutations in the middle domain that potentiate disaggregase activity. Thus, the NTD is critical for the full repertoire of Hsp104 activities. äMechanistic and structural insights into the prion-disaggregase activi(epmc).pdf DeepDyve Pubget Overpricing