Literature DB >> 23273742

A dancer caught midstep: the structure of ATP-bound Hsp70.

Rui Sousa1.   

Abstract

Hsp70 ATP binding induces substrate release, but the transiency of this state has inhibited its characterization. In this issue, Kityk et al. determine the Hsp70(∗)ATP structure utilizing engineered disulfide bonds, providing insights into the workings of this essential molecular machine.
Copyright © 2012 Elsevier Inc. All rights reserved.

Entities:  

Year:  2012        PMID: 23273742      PMCID: PMC3746503          DOI: 10.1016/j.molcel.2012.12.008

Source DB:  PubMed          Journal:  Mol Cell        ISSN: 1097-2765            Impact factor:   17.970


  8 in total

1.  Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions.

Authors:  Moritz Marcinowski; Matthias Höller; Matthias J Feige; Danae Baerend; Don C Lamb; Johannes Buchner
Journal:  Nat Struct Mol Biol       Date:  2011-01-09       Impact factor: 15.369

2.  Structural basis of J cochaperone binding and regulation of Hsp70.

Authors:  Jianwen Jiang; E Guy Maes; Alexander B Taylor; Liping Wang; Andrew P Hinck; Eileen M Lafer; Rui Sousa
Journal:  Mol Cell       Date:  2007-11-09       Impact factor: 17.970

3.  Mechanics of Hsp70 chaperones enables differential interaction with client proteins.

Authors:  Rainer Schlecht; Annette H Erbse; Bernd Bukau; Matthias P Mayer
Journal:  Nat Struct Mol Biol       Date:  2011-01-30       Impact factor: 15.369

4.  Structural analysis of substrate binding by the molecular chaperone DnaK.

Authors:  X Zhu; X Zhao; W F Burkholder; A Gragerov; C M Ogata; M E Gottesman; W A Hendrickson
Journal:  Science       Date:  1996-06-14       Impact factor: 47.728

5.  Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones.

Authors:  Roman Kityk; Jürgen Kopp; Irmgard Sinning; Matthias P Mayer
Journal:  Mol Cell       Date:  2012-11-01       Impact factor: 17.970

6.  Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states.

Authors:  Joanna F Swain; Edda G Schulz; Lila M Gierasch
Journal:  J Biol Chem       Date:  2005-11-06       Impact factor: 5.157

7.  Kinetics of molecular chaperone action.

Authors:  D Schmid; A Baici; H Gehring; P Christen
Journal:  Science       Date:  1994-02-18       Impact factor: 47.728

8.  Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.

Authors:  Eric B Bertelsen; Lyra Chang; Jason E Gestwicki; Erik R P Zuiderweg
Journal:  Proc Natl Acad Sci U S A       Date:  2009-05-13       Impact factor: 11.205

  8 in total
  4 in total

Review 1.  The chaperone toolbox at the single-molecule level: From clamping to confining.

Authors:  Mario J Avellaneda; Eline J Koers; Mohsin M Naqvi; Sander J Tans
Journal:  Protein Sci       Date:  2017-04-20       Impact factor: 6.725

2.  Putative model for heat shock protein 70 complexation with receptor of advanced glycation end products through fluorescence proximity assays and normal mode analyses.

Authors:  Marcelo Sartori Grunwald; Rodrigo Ligabue-Braun; Cristiane Santos Souza; Luana Heimfarth; Hugo Verli; Daniel Pens Gelain; José Cláudio Fonseca Moreira
Journal:  Cell Stress Chaperones       Date:  2016-11-17       Impact factor: 3.667

3.  Mutations in the substrate binding site of human heat-shock protein 70 indicate specific interaction with HLA-DR outside the peptide binding groove.

Authors:  Karin M Rohrer; Markus Haug; Daniela Schwörer; Hubert Kalbacher; Ursula Holzer
Journal:  Immunology       Date:  2014-06       Impact factor: 7.397

Review 4.  Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones.

Authors:  Andrija Finka; Sandeep K Sharma; Pierre Goloubinoff
Journal:  Front Mol Biosci       Date:  2015-06-05
  4 in total

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