scholarly journals Binding Specificity of an α-Helical Protein Sequence to a Full-Length Hsp70 Chaperone and Its Minimal Substrate-Binding Domain†

Biochemistry ◽  
2006 ◽  
Vol 45 (46) ◽  
pp. 13835-13846 ◽  
Author(s):  
Carolina A. Vega ◽  
Neşe Kurt ◽  
Zhongjing Chen ◽  
Stefan Rüdiger ◽  
Silvia Cavagnero
Keyword(s):  
Protein Sequence ◽  
Substrate Binding ◽  
Binding Specificity ◽  
Binding Domain ◽  
Full Length ◽  
Hsp70 Chaperone ◽  
Helical Protein ◽  
Substrate Binding Domain

Solvent Interaction of a Hsp70 Chaperone Substrate-Binding Domain Investigated with Water−NOE NMR Experiments†

Biochemistry ◽  
2003 ◽  
Vol 42 (38) ◽  
pp. 11100-11108 ◽  
Author(s):  
Sheng Cai ◽  
Shawn Y. Stevens ◽  
Andrew P. Budor ◽  
Erik R. P. Zuiderweg
Keyword(s):  
Substrate Binding ◽  
Binding Domain ◽  
Solvent Interaction ◽  
Hsp70 Chaperone ◽  
Substrate Binding Domain

Defining the structure of the substrate-free state of the DnaK molecular chaperone

2001 ◽  
Vol 68 ◽  
pp. 69-82 ◽  
Author(s):  
Joanna F. Swain ◽  
Renuka Sivendran ◽  
Lila M. Gierasch
Keyword(s):  
Binding Site ◽  
Substrate Binding ◽  
Binding Domain ◽  
Full Length ◽  
Free State ◽  
Substrate Binding Site ◽  
Terminal Domain ◽  
C Terminus ◽  
Ph Dependent ◽  
Substrate Binding Domain

Members of the Hsp70 (heat-shock protein of 70 kDa) family of molecular chaperones bind to exposed hydrophobic stretches on substrate proteins in order to dissociate molecular complexes and prevent aggregation in the cell. Substrate affinity for the C-terminal domain of the Hsp70 is regulated by ATP binding to the N-terminal domain utilizing an allosteric mechanism. Our multi-dimensional NMR studies of a substrate-binding domain fragment (amino acids 387-552) from an Escherichia coli Hsp70, DnaK(387-552), have uncovered a pH-dependent conformational change, which we propose to be relevant for the full-length protein also. At pH 7, the C-terminus of DnaK(387-552) mimics substrate by binding to its own substrate-binding site, as has been observed previously for truncated Hsp70 constructs. At pH 5, the C-terminus is released from the binding site, such that DnaK is in the substrate-free state 10-20% of the time. We propose that the mechanism for the release of the tail is a loss of affinity for substrate at low pH. The pH-dependent fluorescence changes at a tryptophan residue near the substrate-binding pocket in full-length DnaK lead us to extend these conclusions to the full-length DnaK as well. In the context of the DnaK substrate-binding domain fragment, the release of the C-terminus from the substrate-binding site provides our first glimpse of the empty conformation of an Hsp70 substrate-binding domain containing a portion of the helical subdomain.

scholarly journals Entropic Inhibition: How the Activity of a AAA+ Machine Is Modulated by Its Substrate-Binding Domain

2021 ◽  
Author(s):  
Marija Iljina ◽  
Hisham Mazal ◽  
Pierre Goloubinoff ◽  
Inbal Riven ◽  
Gilad Haran
Keyword(s):  
Substrate Binding ◽  
Binding Domain ◽  
Substrate Binding Domain

scholarly journals Flexible Linkers Leash the Substrate Binding Domain of SspB to a Peptide Module that Stabilizes Delivery Complexes with the AAA+ ClpXP Protease

2003 ◽  
Vol 12 (2) ◽  
pp. 355-363 ◽  
Author(s):  
David A Wah ◽  
Igor Levchenko ◽  
Gabrielle E Rieckhof ◽  
Daniel N Bolon ◽  
Tania A Baker ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Binding Domain ◽  
Substrate Binding Domain

scholarly journals An atomistic view of Hsp70 allosteric crosstalk: from the nucleotide to the substrate binding domain and back

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Federica Chiappori ◽  
Ivan Merelli ◽  
Luciano Milanesi ◽  
Giorgio Colombo ◽  
Giulia Morra
Keyword(s):  
Substrate Binding ◽  
Binding Domain ◽  
Substrate Binding Domain

Rotary and Unidirectional Metal Shadowing of VAT: Localization of the Substrate-Binding Domain

2000 ◽  
Vol 132 (2) ◽  
pp. 162-168 ◽  
Author(s):  
Beate Rockel ◽  
Reinhard Guckenberger ◽  
Heinz Gross ◽  
Peter Tittmann ◽  
Wolfgang Baumeister
Keyword(s):  
Substrate Binding ◽  
Binding Domain ◽  
Substrate Binding Domain

Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide

2019 ◽  
Vol 124 ◽  
pp. 111-120 ◽  
Author(s):  
Ana O. Tiroli-Cepeda ◽  
Thiago V. Seraphim ◽  
Glaucia M.S. Pinheiro ◽  
Denio E.P. Souto ◽  
Lauro T. Kubota ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Binding Domain ◽  
J Domain ◽  
Substrate Binding Domain

Engineering the substrate-binding domain of an esterase enhances its hydrolytic activity toward fatty acid esters

2014 ◽  
Vol 49 (12) ◽  
pp. 2101-2106 ◽  
Author(s):  
Young-A Lee ◽  
Eun-Yeong Jeon ◽  
Sun-Mee Lee ◽  
Uwe T. Bornscheuer ◽  
Jin-Byung Park
Keyword(s):  
Fatty Acid ◽  
Substrate Binding ◽  
Hydrolytic Activity ◽  
Binding Domain ◽  
Fatty Acid Esters ◽  
Substrate Binding Domain ◽  
Acid Esters

Identification of Hsp70 modulators through modeling of the substrate binding domain

2009 ◽  
Vol 19 (14) ◽  
pp. 3828-3831 ◽  
Author(s):  
Conor M. Haney ◽  
Corinne Schneider ◽  
Barbara Beck ◽  
Jeffrey L. Brodsky ◽  
Alexander Dömling
Keyword(s):  
Substrate Binding ◽  
Binding Domain ◽  
Substrate Binding Domain
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