Literature DB >> 8637005

Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure.

A Aharoni1, A Horovitz.   

Abstract

The crystal structures of the chaperonin GroEL Arg13 --> Gly; Ala126 --> Val double mutant, without and in complex with ATP gamma S, have been determined at atomic resolution. Here, we show that the double mutation Arg13 --> Gly; Ala126 --> Val disrupts negative co-operativity between GroEL rings, with respect to ATP, but has little effect on the positive co-operativity within each ring. Our results help to explain why the double mutation facilitated the crystallization of GroEL and why breaking of dyad symmetry between rings is not observed in crystal structures of this mutant. Our results may also help to explain why the observed structural differences between the GroEL double mutant and its ATP gamma S-bound form are small.

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Year:  1996        PMID: 8637005     DOI: 10.1006/jmbi.1996.0282

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  12 in total

1.  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

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

Authors:  Stefanie Reissmann; Charles Parnot; Christopher R Booth; Wah Chiu; Judith Frydman
Journal:  Nat Struct Mol Biol       Date:  2007-04-29       Impact factor: 15.369

3.  Atomic force microscopy detects changes in the interaction forces between GroEL and substrate proteins.

Authors:  A Vinckier; P Gervasoni; F Zaugg; U Ziegler; P Lindner; P Groscurth; A Plückthun; G Semenza
Journal:  Biophys J       Date:  1998-06       Impact factor: 4.033

Review 4.  The versatile mutational "repertoire" of Escherichia coli GroEL, a multidomain chaperonin nanomachine.

Authors:  Tomohiro Mizobata; Yasushi Kawata
Journal:  Biophys Rev       Date:  2017-11-27

5.  The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex.

Authors:  P Lin; F Sherman
Journal:  Proc Natl Acad Sci U S A       Date:  1997-09-30       Impact factor: 11.205

6.  Analysis of mutationally altered forms of the Cct6 subunit of the chaperonin from Saccharomyces cerevisiae.

Authors:  P Lin; T S Cardillo; L M Richard; G B Segel; F Sherman
Journal:  Genetics       Date:  1997-12       Impact factor: 4.562

7.  Coupling between protein folding and allostery in the GroE chaperonin system.

Authors:  O Yifrach; A Horovitz
Journal:  Proc Natl Acad Sci U S A       Date:  2000-02-15       Impact factor: 11.205

8.  Spontaneous conformational changes in the E. coli GroEL subunit from all-atom molecular dynamics simulations.

Authors:  Yelena Sliozberg; Cameron F Abrams
Journal:  Biophys J       Date:  2007-05-18       Impact factor: 4.033

9.  Markov propagation of allosteric effects in biomolecular systems: application to GroEL-GroES.

Authors:  Chakra Chennubhotla; Ivet Bahar
Journal:  Mol Syst Biol       Date:  2006-07-04       Impact factor: 11.429

10.  Integration of evolutionary features for the identification of functionally important residues in major facilitator superfamily transporters.

Authors:  Jouhyun Jeon; Jae-Seong Yang; Sanguk Kim
Journal:  PLoS Comput Biol       Date:  2009-10-02       Impact factor: 4.475

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