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Literature DB >> 11868280

Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding.

H R Saibil¹, A L Horwich, W A Fenton.

Abstract

Entities: Gene

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Year: 2001 PMID： 11868280 DOI： 10.1016/s0065-3233(01)59002-6

Source DB: PubMed Journal: Adv Protein Chem ISSN： 0065-3233

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14 in total

1. The unfolding action of GroEL on a protein substrate.

Authors: Arjan van der Vaart; Jianpeng Ma; Martin Karplus
Journal: Biophys J Date: 2004-07 Impact factor: 4.033

2. Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 -> Ala.

Authors: Oded Danziger; Dalia Rivenzon-Segal; Sharon G Wolf; Amnon Horovitz
Journal: Proc Natl Acad Sci U S A Date: 2003-11-13 Impact factor: 11.205

3. Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.

Authors: Jose H Pereira; Corie Y Ralston; Nicholai R Douglas; Daniel Meyer; Kelly M Knee; Daniel R Goulet; Jonathan A King; Judith Frydman; Paul D Adams
Journal: J Biol Chem Date: 2010-06-23 Impact factor: 5.157

Review 4. First glimpses of a chaperonin-bound folding intermediate.

Authors: Joanna F Swain; Lila M Gierasch
Journal: Proc Natl Acad Sci U S A Date: 2005-09-19 Impact factor: 11.205

5. Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis.

Authors: Oded Danziger; Liat Shimon; Amnon Horovitz
Journal: Protein Sci Date: 2006-05-02 Impact factor: 6.725

6. Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner.

Authors: Yakov Kipnis; Niv Papo; Gilad Haran; Amnon Horovitz
Journal: Proc Natl Acad Sci U S A Date: 2007-02-21 Impact factor: 11.205

Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding.

1. The unfolding action of GroEL on a protein substrate.

2. Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 -> Ala.

3. Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.

Review 4. First glimpses of a chaperonin-bound folding intermediate.

5. Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis.

6. Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner.

7. Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins.

8. Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.

9. Setting the chaperonin timer: a two-stroke, two-speed, protein machine.

10. Concerted release of substrate domains from GroEL by ATP is demonstrated with FRET.