Literature DB >> 2143562

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein.

K M Flaherty1, C DeLuca-Flaherty, D B McKay.   

Abstract

The three-dimensional structure of the amino-terminal 44K ATPase fragment of the 70K bovine heat-shock cognate protein has been solved to a resolution of 2.2 A. The ATPase fragment has two structural lobes with a deep cleft between them; ATP binds at the base of the cleft. Surprisingly, the nucleotide-binding 'core' of the ATPase fragment has a tertiary structure similar to that of hexokinase, although the remainder of the structures of the two proteins are completely dissimilar, suggesting that both the phosphotransferase mechanism and the substrate-induced conformational change intrinsic to the hexokinases may be used by the 70K heat shock-related proteins.

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Year:  1990        PMID: 2143562     DOI: 10.1038/346623a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  299 in total

1.  Intragenic suppressors of Hsp70 mutants: interplay between the ATPase- and peptide-binding domains.

Authors:  J E Davis; C Voisine; E A Craig
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-03       Impact factor: 11.205

2.  HSP70 homolog functions in cell-to-cell movement of a plant virus.

Authors:  V V Peremyslov; Y Hagiwara; V V Dolja
Journal:  Proc Natl Acad Sci U S A       Date:  1999-12-21       Impact factor: 11.205

3.  Crystal structure of the cell division protein FtsA from Thermotoga maritima.

Authors:  F van den Ent; J Löwe
Journal:  EMBO J       Date:  2000-10-16       Impact factor: 11.598

4.  Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outer membrane protein disulfide bonds.

Authors:  Jane E Raulston; Carolyn H Davis; Terry R Paul; J Dave Hobbs; Priscilla B Wyrick
Journal:  Infect Immun       Date:  2002-02       Impact factor: 3.441

5.  Cell-to-cell movement and assembly of a plant closterovirus: roles for the capsid proteins and Hsp70 homolog.

Authors:  D V Alzhanova; A J Napuli; R Creamer; V V Dolja
Journal:  EMBO J       Date:  2001-12-17       Impact factor: 11.598

6.  Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s.

Authors:  C Pfund; P Huang; N Lopez-Hoyo; E A Craig
Journal:  Mol Biol Cell       Date:  2001-12       Impact factor: 4.138

Review 7.  Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.

Authors:  Franz Narberhaus
Journal:  Microbiol Mol Biol Rev       Date:  2002-03       Impact factor: 11.056

8.  ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release.

Authors:  T K Barthel; J Zhang; G C Walker
Journal:  J Bacteriol       Date:  2001-10       Impact factor: 3.490

9.  Nucleolar targeting of the chaperone hsc70 is regulated by stress, cell signaling, and a composite targeting signal which is controlled by autoinhibition.

Authors:  Piotr Bański; Hicham Mahboubi; Mohamed Kodiha; Sanhita Shrivastava; Cynthia Kanagaratham; Ursula Stochaj
Journal:  J Biol Chem       Date:  2010-05-10       Impact factor: 5.157

Review 10.  The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum.

Authors:  Addmore Shonhai; Aileen Boshoff; Gregory L Blatch
Journal:  Protein Sci       Date:  2007-09       Impact factor: 6.725

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